|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
18-418 |
0e+00 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 737.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 18 EEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTWMKD 97
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 98 EPVSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFA 177
Cdd:cd07132 81 EPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 178 VMLGGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTC 257
Cdd:cd07132 161 VVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 258 VAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGGQSDEGERYIAPTVLVDV 337
Cdd:cd07132 241 IAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 338 QETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLSSLPFGG 417
Cdd:cd07132 321 KPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGG 400
|
.
gi 569005993 418 V 418
Cdd:cd07132 401 V 401
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
21-418 |
0e+00 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 628.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 21 LQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTWMKDEPV 100
Cdd:cd07087 4 VARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 101 STNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVML 180
Cdd:cd07087 84 SVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 181 GGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAP 260
Cdd:cd07087 164 GGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 261 DYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGGQSDEGERYIAPTVLVDVQET 340
Cdd:cd07087 244 DYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDVSPD 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569005993 341 EPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLSSLPFGGV 418
Cdd:cd07087 324 SPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGV 401
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
18-418 |
0e+00 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 570.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 18 EEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTWMKD 97
Cdd:cd07136 1 ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 98 EPVSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFA 177
Cdd:cd07136 81 KRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 178 VMLGGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTC 257
Cdd:cd07136 161 VVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 258 VAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGGQSDEGERYIAPTVLVDV 337
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 338 QETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLSSLPFGG 417
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGG 400
|
.
gi 569005993 418 V 418
Cdd:cd07136 401 V 401
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
14-418 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 562.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 14 TDPFEEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQT 93
Cdd:PTZ00381 6 PEIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 94 WMKDEPVSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQ 173
Cdd:PTZ00381 86 YLKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 174 SCFAVMLGGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA 253
Cdd:PTZ00381 166 SYVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 254 GQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGC--GRVAIGGQSDEGERYIAP 331
Cdd:PTZ00381 246 GQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDhgGKVVYGGEVDIENKYVAP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 332 TVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLS 411
Cdd:PTZ00381 326 TIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNP 405
|
....*..
gi 569005993 412 SLPFGGV 418
Cdd:PTZ00381 406 NLPFGGV 412
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
15-418 |
0e+00 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 537.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 15 DPFEEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTW 94
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 95 MKDEPVSTNLLT-KLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQ 173
Cdd:cd07135 85 AKDEKVKDGPLAfMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 174 SCFAVMLGGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA 253
Cdd:cd07135 165 DAFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 254 GQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGC--GRVAIGGQSDEGERYIAP 331
Cdd:cd07135 245 GQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTtkGKVVIGGEMDEATRFIPP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 332 TVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLS 411
Cdd:cd07135 325 TIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVD 404
|
....*..
gi 569005993 412 SLPFGGV 418
Cdd:cd07135 405 NAPFGGV 411
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
32-418 |
3.88e-163 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 466.70 E-value: 3.88e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 32 KTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTWMKDEPVSTNLLTKLSTA 111
Cdd:cd07134 15 RASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTPLLLFGTKS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 112 FIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPEETGQLLE 191
Cdd:cd07134 95 KIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAEVAQALLE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 192 HKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQE 271
Cdd:cd07134 175 LPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 272 QLVPALQNAITRFYGDNPQT--SPNLGRIINQKHFKRLQGLL-----GCGRVAIGGQSDEGERYIAPTVLVDVQETEPVM 344
Cdd:cd07134 255 AFVEHLKAEIEKFYGKDAARkaSPDLARIVNDRHFDRLKGLLddavaKGAKVEFGGQFDAAQRYIAPTVLTNVTPDMKIM 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569005993 345 QEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLSSLPFGGV 418
Cdd:cd07134 335 QEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGV 408
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
18-418 |
9.82e-163 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 465.73 E-value: 9.82e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 18 EEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTWMKD 97
Cdd:cd07137 2 PRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 98 EPVSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFA 177
Cdd:cd07137 82 EKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 178 VMLGGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRY-FNAGQT 256
Cdd:cd07137 162 VIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 257 CVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAI----GGQSDEGERYIAPT 332
Cdd:cd07137 242 CIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADkivhGGERDEKNLYIEPT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 333 VLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLSS 412
Cdd:cd07137 322 ILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDT 401
|
....*.
gi 569005993 413 LPFGGV 418
Cdd:cd07137 402 LPFGGV 407
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
21-418 |
4.38e-152 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 438.46 E-value: 4.38e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 21 LQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLG-KSGFESDMSEIILCENEVDLALKNLQTWMKDEP 99
Cdd:cd07133 4 LERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLLAEILPSIAGIKHARKHLKKWMKPSR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 100 VSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVM 179
Cdd:cd07133 84 RHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 180 LGGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVA 259
Cdd:cd07133 164 TGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 260 PDYILCSQEMQEQLVPALQNAITRFYGDnPQTSPNLGRIINQKHFKRLQGLL------GCGRVAIG--GQSDEGERYIAP 331
Cdd:cd07133 244 PDYVLVPEDKLEEFVAAAKAAVAKMYPT-LADNPDYTSIINERHYARLQGLLedarakGARVIELNpaGEDFAATRKLPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 332 TVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLS 411
Cdd:cd07133 323 TLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQD 402
|
....*..
gi 569005993 412 SLPFGGV 418
Cdd:cd07133 403 DLPFGGV 409
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
18-418 |
4.72e-139 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 407.19 E-value: 4.72e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 18 EEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTWMKD 97
Cdd:PLN02203 9 EGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMAP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 98 EPVSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFA 177
Cdd:PLN02203 89 KKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 178 VMLGGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVD---DNCDPQTVANRVAWFRYFN-A 253
Cdd:PLN02203 169 VIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 254 GQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAI----GGQSDEGERYI 329
Cdd:PLN02203 249 GQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAAsivhGGSIDEKKLFI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 330 APTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMT 409
Cdd:PLN02203 329 EPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYA 408
|
....*....
gi 569005993 410 LSSLPFGGV 418
Cdd:PLN02203 409 CDSLPFGGV 417
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
18-418 |
1.77e-119 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 355.36 E-value: 1.77e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 18 EEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMsEIILCENEVDLALKNLQTWMKD 97
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 98 EPVSTNLLTKlstAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCF 176
Cdd:cd07078 80 VIPSPDPGEL---AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 177 AVMLGGPEETGQ-LLEH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAG 254
Cdd:cd07078 157 NVVTGDGDEVGAaLASHpRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 255 QTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNP-QTSPNLGRIINQKHFKRLQGLL-----GCGRVAIGGQSDEGE-- 326
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPlDPDTDMGPLISAAQLDRVLAYIedakaEGAKLLCGGKRLEGGkg 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 327 RYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFM 406
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410
....*....|..
gi 569005993 407 YMTlSSLPFGGV 418
Cdd:cd07078 397 GAE-PSAPFGGV 407
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
24-419 |
2.39e-106 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 323.54 E-value: 2.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 24 LKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTWMKDEPVSTN 103
Cdd:PLN02174 19 LRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 104 LLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGP 183
Cdd:PLN02174 99 LTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 184 EETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRY-FNAGQTCVAPDY 262
Cdd:PLN02174 179 TETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 263 ILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLG----CGRVAIGGQSDEGERYIAPTVLVDVQ 338
Cdd:PLN02174 259 ILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPTILLDVP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 339 ETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLSSLPFGGV 418
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGV 418
|
.
gi 569005993 419 A 419
Cdd:PLN02174 419 G 419
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
25-418 |
2.84e-92 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 283.35 E-value: 2.84e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 25 KEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMsEIILCENEVDLALKNLQTWMKDEPVSTNL 104
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 105 LTKlstAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGP 183
Cdd:cd06534 83 GGE---AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 184 EETGQ-LLEH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD 261
Cdd:cd06534 160 DEVGAaLLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 262 YILCSQEMQEQLVPALQnaitrfygdnpqtspnlgriinqkhfkrlqgllgcgrvaiggqsdegeryiapTVLVDVQETE 341
Cdd:cd06534 240 RLLVHESIYDEFVEKLV-----------------------------------------------------TVLVDVDPDM 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569005993 342 PVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLsSLPFGGV 418
Cdd:cd06534 267 PIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGP-EAPFGGV 342
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
25-418 |
6.17e-89 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 278.55 E-value: 6.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 25 KEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMseiilcenEVDLALKNLQTW------MKDE 98
Cdd:COG1012 53 RAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARG--------EVDRAADFLRYYagearrLYGE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 99 pvSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFA 177
Cdd:COG1012 125 --TIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 178 VMLGGPEETGQ-LLEH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQ 255
Cdd:COG1012 203 VVTGDGSEVGAaLVAHpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQ 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 256 TCVAPDYILCSQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLLGCG-----RVAIGGQSDEGER-- 327
Cdd:COG1012 283 RCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIEDAvaegaELLTGGRRPDGEGgy 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 328 YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMY 407
Cdd:COG1012 363 FVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTG 442
|
410
....*....|.
gi 569005993 408 MTLsSLPFGGV 418
Cdd:COG1012 443 AVP-QAPFGGV 452
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
25-418 |
1.63e-83 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 264.01 E-value: 1.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 25 KEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESdMSEIILCENEVDLALKNLQTwMKDEPVSTnl 104
Cdd:pfam00171 39 RAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEA-RGEVDRAIDVLRYYAGLARR-LDGETLPS-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 105 lTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGP 183
Cdd:pfam00171 115 -DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgLPAGVLNVVTGSG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 184 EETGQ-LLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD 261
Cdd:pfam00171 194 AEVGEaLVEHPdVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 262 YILCSQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLL-----GCGRVAIGGQSDEGE-RYIAPTVL 334
Cdd:pfam00171 274 RLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAGLDNgYFVEPTVL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 335 VDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYmTLSSLP 414
Cdd:pfam00171 354 ANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTG-DADGLP 432
|
....
gi 569005993 415 FGGV 418
Cdd:pfam00171 433 FGGF 436
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
39-418 |
7.10e-80 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 254.45 E-value: 7.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 39 RAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESdMSEIILCENEVDLALKNLQTWMKDEPVSTNLLTKLSTAFIRKEPF 118
Cdd:cd07099 42 RAQRLLRWKRALADHADELAELLHAETGKPRADA-GLEVLLALEAIDWAARNAPRVLAPRKVPTGLLMPNKKATVEYRPY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 119 GLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGpEETGQ-LLEHKFDY 196
Cdd:cd07099 121 GVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAgPPQGVLQVVTGD-GATGAaLIDAGVDK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 197 IFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQEQLVPA 276
Cdd:cd07099 200 VAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVAR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 277 L--------QNAITRFYGD-NPQTSPNLGRIInQKHFKrlQGLLGCGRVAIGG-QSDEGERYIAPTVLVDVQETEPVMQE 346
Cdd:cd07099 280 LvakaralrPGADDIGDADiGPMTTARQLDIV-RRHVD--DAVAKGAKALTGGaRSNGGGPFYEPTVLTDVPHDMDVMRE 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569005993 347 EIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLSSLPFGGV 418
Cdd:cd07099 357 ETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGV 428
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
18-418 |
1.13e-67 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 222.95 E-value: 1.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 18 EEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTWMKD 97
Cdd:cd07098 21 DEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 98 EPVSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEIS--------KNTEKVLAEL-LP 168
Cdd:cd07098 101 ESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVawssgfflSIIRECLAACgHD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 169 QYLDQSCFavmlGGPEETGQLLEH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANrvAW 247
Cdd:cd07098 181 PDLVQLVT----CLPETAEALTSHpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIAS--II 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 248 FR--YFNAGQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNP-QTSPNLGRIINQKHFKRLQGLLG----------CG 314
Cdd:cd07098 255 MRgtFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPlDGDVDVGAMISPARFDRLEELVAdavekgarllAG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 315 RVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLART 394
Cdd:cd07098 335 GKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQL 414
|
410 420
....*....|....*....|....*
gi 569005993 395 SSGGFCGND-GFMYMtLSSLPFGGV 418
Cdd:cd07098 415 ETGMVAINDfGVNYY-VQQLPFGGV 438
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
25-417 |
1.37e-65 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 217.19 E-value: 1.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 25 KEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGK---SGFESDMSEIILCENEVDLALKNLQTwmkdePVS 101
Cdd:cd07092 29 HAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKplhLVRDDELPGAVDNFRFFAGAARTLEG-----PAA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 102 TNLLTKLsTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLG 181
Cdd:cd07092 104 GEYLPGH-TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 182 GPEETGQLL--EHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVA 259
Cdd:cd07092 183 GGASAGDALvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 260 PDYILCSQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLL----GCGRVAIGGQSDEGERY-IAPTV 333
Cdd:cd07092 263 ACRVYVHESVYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVerapAHARVLTGGRRAEGPGYfYEPTV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 334 LVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYmtLSSL 413
Cdd:cd07092 343 VAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIPL--AAEM 420
|
....
gi 569005993 414 PFGG 417
Cdd:cd07092 421 PHGG 424
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
112-418 |
2.23e-59 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 200.74 E-value: 2.23e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 112 FIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEETGQ-L 189
Cdd:cd07103 112 LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAgLPAGVLNVVTGSPAEIGEaL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 190 LEH----KfdyIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILC 265
Cdd:cd07103 192 CASprvrK---ISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 266 SQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGL----LGCG-RVAIGGQ-SDEGERYIAPTVLVDVQ 338
Cdd:cd07103 269 HESIYDEFVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEKVEALvedaVAKGaKVLTGGKrLGLGGYFYEPTVLTDVT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 339 ETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSG--GFcgNDGFmyMTLSSLPFG 416
Cdd:cd07103 349 DDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGmvGI--NTGL--ISDAEAPFG 424
|
..
gi 569005993 417 GV 418
Cdd:cd07103 425 GV 426
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
25-417 |
3.57e-59 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 200.55 E-value: 3.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 25 KEAFNTGKTKT-AKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKS-GFESDMseiilcenEVDLALKNLQTW-----MKD 97
Cdd:cd07089 29 RRAFDTGDWSTdAEERARCLRQLHEALEARKEELRALLVAEVGAPvMTARAM--------QVDGPIGHLRYFadladSFP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 98 EPVS---TNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAEL-----LPq 169
Cdd:cd07089 101 WEFDlpvPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIiaetdLP- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 170 yldQSCFAVMLGGPEETGQLL--EHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAW 247
Cdd:cd07089 180 ---AGVVNVVTGSDNAVGEALttDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 248 FRYFNAGQTCVAPDYILCSQEMQEQLVPALQNAITRF-YGD--NPQTspNLGRIINQKHFKRLQGLLGCGR------VAI 318
Cdd:cd07089 257 VCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALpVGDpaDPGT--VMGPLISAAQRDRVEGYIARGRdegarlVTG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 319 GGQSDEGER--YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSS 396
Cdd:cd07089 335 GGRPAGLDKgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRT 414
|
410 420
....*....|....*....|.
gi 569005993 397 GGFCGNDGFMYMtlSSLPFGG 417
Cdd:cd07089 415 GSVGINGGGGYG--PDAPFGG 433
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
110-418 |
4.34e-59 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 200.15 E-value: 4.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 110 TAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEETGQ 188
Cdd:cd07109 110 FVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGLGAEAGA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 189 -LLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCS 266
Cdd:cd07109 190 aLVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVH 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 267 QEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLL-----GCGRVAIGGQSDEGER----YIAPTVLVDV 337
Cdd:cd07109 270 RSIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVEGFVararaRGARIVAGGRIAEGAPaggyFVAPTLLDDV 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 338 QETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLsSLPFGG 417
Cdd:cd07109 350 PPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGI-ELPFGG 428
|
.
gi 569005993 418 V 418
Cdd:cd07109 429 V 429
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
110-418 |
8.19e-59 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 199.75 E-value: 8.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 110 TAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPEETGQ- 188
Cdd:PRK13473 131 TSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDa 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 189 LLEH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQ 267
Cdd:PRK13473 211 LVGHpKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQR 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 268 EMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGL------LGCGRVAIGGQSDEGE-RYIAPTVLVDVQE 339
Cdd:PRK13473 291 GIYDDLVAKLAAAVATLkVGDPDDEDTELGPLISAAHRDRVAGFverakaLGHIRVVTGGEAPDGKgYYYEPTLLAGARQ 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569005993 340 TEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYmtLSSLPFGGV 418
Cdd:PRK13473 371 DDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFML--VSEMPHGGQ 447
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
113-370 |
6.41e-58 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 196.60 E-value: 6.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 113 IRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVmLGGPEETGQLL-E 191
Cdd:cd07106 110 LRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNV-VSGGDELGPALtS 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 192 H-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQ 270
Cdd:cd07106 189 HpDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIY 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 271 EQLVPALQNAITRFY-GDNPQTSPNLGRIINQKHFKRLQGLL-----GCGRVAIGGQSDEGERY-IAPTVLVDVQETEPV 343
Cdd:cd07106 269 DEFCEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVedakaKGAKVLAGGEPLDGPGYfIPPTIVDDPPEGSRI 348
|
250 260
....*....|....*....|....*..
gi 569005993 344 MQEEIFGPILPLVTVRSLDEAIEFMNQ 370
Cdd:cd07106 349 VDEEQFGPVLPVLKYSDEDEVIARAND 375
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
112-369 |
2.02e-57 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 195.54 E-value: 2.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 112 FIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAEL-----LPQYLdqscFAVMLGGPEET 186
Cdd:cd07102 111 YIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAfaeagLPEGV----FQVLHLSHETS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 187 GQLL-EHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILC 265
Cdd:cd07102 187 AALIaDPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 266 SQEMQEQLVPALQnAITRFY--GDNPQTSPNLGRIINQKHFKRLQGLL------GcGRVAIGGQ----SDEGERYIAPTV 333
Cdd:cd07102 267 HESIYDAFVEAFV-AVVKGYklGDPLDPSTTLGPVVSARAADFVRAQIadaiakG-ARALIDGAlfpeDKAGGAYLAPTV 344
|
250 260 270
....*....|....*....|....*....|....*.
gi 569005993 334 LVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMN 369
Cdd:cd07102 345 LTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMN 380
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
25-397 |
1.10e-55 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 191.03 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 25 KEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFES--DMSEIILC-ENEVDLA--LKNLQtwmkdeP 99
Cdd:cd07110 29 RRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAawDVDDVAGCfEYYADLAeqLDAKA------E 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 100 VSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAEL-----LPQyldqS 174
Cdd:cd07110 103 RAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIaaeagLPP----G 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 175 CFAVMLGGPEETGQ-LLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFN 252
Cdd:cd07110 179 VLNVVTGTGDEAGApLAAHPgIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWN 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 253 AGQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSP-NLGRIINQKHFKRLQGLLGCG-----RVAIGGQSDEGE 326
Cdd:cd07110 259 NGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGvRLGPLVSQAQYEKVLSFIARGkeegaRLLCGGRRPAHL 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569005993 327 R---YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSG 397
Cdd:cd07110 339 EkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAG 412
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
110-393 |
1.40e-55 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 191.32 E-value: 1.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 110 TAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAEL-----LPQYLdqscFAVMLGGPE 184
Cdd:cd07088 126 NIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELvdeagLPAGV----LNIVTGRGS 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 185 ETGQLL-EH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 262
Cdd:cd07088 202 VVGDALvAHpKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAER 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 263 ILCSQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLL------GcGRVAIGGQSDEGER--YIAPTV 333
Cdd:cd07088 282 VYVHEDIYDEFMEKLVEKMKAVkVGDPFDAATDMGPLVNEAALDKVEEMVeraveaG-ATLLTGGKRPEGEKgyFYEPTV 360
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 334 LVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLAR 393
Cdd:cd07088 361 LTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNE 420
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
110-418 |
4.01e-55 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 189.47 E-value: 4.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 110 TAFIRKEPFGLVLIIAPWNYPvnLMIIP--LVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEET 186
Cdd:cd07118 112 LGLVLREPIGVVGIITPWNFP--FLILSqkLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGYGATV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 187 GQ-LLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYIL 264
Cdd:cd07118 190 GQaMTEHPdVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 265 CSQEMQEQLVPALQnAITRF--YGD--NPQTspNLGRIINQKHFKRLQGLLGCGR-----VAIGGQSDEGE--RYIAPTV 333
Cdd:cd07118 270 VHESIADAFVAAVV-ARSRKvrVGDplDPET--KVGAIINEAQLAKITDYVDAGRaegatLLLGGERLASAagLFYQPTI 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 334 LVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGN---DGFmymtl 410
Cdd:cd07118 347 FTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNtflDGS----- 421
|
....*...
gi 569005993 411 SSLPFGGV 418
Cdd:cd07118 422 PELPFGGF 429
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
106-417 |
1.85e-54 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 188.10 E-value: 1.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 106 TKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAEL-----LPqyldQSCFAVML 180
Cdd:cd07138 119 ERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEIldeagLP----AGVFNLVN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 181 GGPEETGQLL-EH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCD-----PQTVANrvawfRYFNA 253
Cdd:cd07138 195 GDGPVVGEALsAHpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADlekavPRGVAA-----CFANS 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 254 GQTCVAPDYILCSQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLLGCG-----RVAIGG-QSDEG- 325
Cdd:cd07138 270 GQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYvVGDPRDPATTLGPLASAAQFDRVQGYIQKGieegaRLVAGGpGRPEGl 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 326 ER--YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGND 403
Cdd:cd07138 350 ERgyFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHING 429
|
330
....*....|....
gi 569005993 404 GFMYMtlsSLPFGG 417
Cdd:cd07138 430 AAFNP---GAPFGG 440
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
39-418 |
1.24e-53 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 185.04 E-value: 1.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 39 RAEQLQSLGRFLQDNSKQLHDALDGDLG----KSGFESDMSEIILCEnevdlALkNLQTWMKDEPVSTNLLTKLSTAfiR 114
Cdd:cd07104 24 RAAILRKAAEILEERRDEIADWLIRESGstrpKAAFEVGAAIAILRE-----AA-GLPRRPEGEILPSDVPGKESMV--R 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 115 KEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSE---ISKNTekVLAEL-----LPQYLdqscFAVMLGGPEET 186
Cdd:cd07104 96 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSrtpVTGGL--LIAEIfeeagLPKGV----LNVVPGGGSEI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 187 GQ-LLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYIL 264
Cdd:cd07104 170 GDaLVEHPrVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRIL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 265 CSQEMQEQLVPALQNAITRF-YGD--NPQTSpnLGRIINQKHFKRLQGLL------GcGRVAIGGQSDegERYIAPTVLV 335
Cdd:cd07104 250 VHESVYDEFVEKLVAKAKALpVGDprDPDTV--IGPLINERQVDRVHAIVedavaaG-ARLLTGGTYE--GLFYQPTVLS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 336 DVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDgfmyMTLSS--- 412
Cdd:cd07104 325 DVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND----QTVNDeph 400
|
....*.
gi 569005993 413 LPFGGV 418
Cdd:cd07104 401 VPFGGV 406
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
111-383 |
1.54e-52 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 182.95 E-value: 1.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 111 AFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPEETGQ-L 189
Cdd:cd07108 111 TYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNVITGYGEECGAaL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 190 LEH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYV--DDNCDpQTVANRVAWFRYFNAGQTCVAPDYILCS 266
Cdd:cd07108 191 VDHpDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVfpDADLD-DAVDGAIAGMRFTRQGQSCTAGSRLFVH 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 267 QEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLLGCG------RVAIGGQSDEGER-----YIAPTVL 334
Cdd:cd07108 270 EDIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIDLGlstsgaTVLRGGPLPGEGPladgfFVQPTIF 349
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 569005993 335 VDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNN 383
Cdd:cd07108 350 SGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
109-418 |
1.13e-51 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 180.49 E-value: 1.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 109 STAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAEL-----LPqyldQSCFAVMLGGP 183
Cdd:cd07112 116 ALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLP----AGVLNVVPGFG 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 184 EETGQLL-EHK-FDYIFFTGSPRVGKIVMTAAAK-HLTPITLELGGKNPCYVDDNC-DPQTVANRVAWFRYFNAGQTCVA 259
Cdd:cd07112 192 HTAGEALgLHMdVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 260 PDYILCSQEMQEQLVPALQNAITRFY-GD--NPQTSpnLGRIINQKHFKRLQGLLGCG-----RVAIGGQS---DEGERY 328
Cdd:cd07112 272 GSRLLVHESIKDEFLEKVVAAAREWKpGDplDPATR--MGALVSEAHFDKVLGYIESGkaegaRLVAGGKRvltETGGFF 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 329 IAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGF---CGNDGF 405
Cdd:cd07112 350 VEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVwvnCFDEGD 429
|
330
....*....|...
gi 569005993 406 MymtlsSLPFGGV 418
Cdd:cd07112 430 I-----TTPFGGF 437
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
5-418 |
2.43e-51 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 180.24 E-value: 2.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 5 GKHPRADQgtDPFEEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFES--DMSEIILCen 82
Cdd:cd07131 29 GTFPLSTA--SDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGrgDVQEAIDM-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 83 eVDLALKNLQTwMKDEPVSTNLLTKLstAFIRKEPFGLVLIIAPWNYPvnlMIIP---LVGAIAAGNCVVLKPSEISKNT 159
Cdd:cd07131 105 -AQYAAGEGRR-LFGETVPSELPNKD--AMTRRQPIGVVALITPWNFP---VAIPswkIFPALVCGNTVVFKPAEDTPAC 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 160 EKVLAELLPQY-LDQSCFAVMLGGPEETGQ-LLEH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNC 236
Cdd:cd07131 178 ALKLVELFAEAgLPPGVVNVVHGRGEEVGEaLVEHpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 237 DPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNL-GRIINQKHFKRLQG------ 309
Cdd:cd07131 258 DLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDmGPLINEAQLEKVLNyneigk 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 310 -----LLGCGRVAIGGQSDEGeRYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNA 384
Cdd:cd07131 338 eegatLLLGGERLTGGGYEKG-YFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDV 416
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 569005993 385 EVIKQVLARTSSggfcgndGFMYMTLSS------LPFGGV 418
Cdd:cd07131 417 NKAFRARRDLEA-------GITYVNAPTigaevhLPFGGV 449
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
111-418 |
6.98e-51 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 178.31 E-value: 6.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 111 AFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEETG-Q 188
Cdd:cd07145 117 AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVGdE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 189 LLEH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQ 267
Cdd:cd07145 197 IVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 268 EMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLL------GcGRVAIGGQSDEGErYIAPTVLVDVQET 340
Cdd:cd07145 277 EVYDKFLKLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMENLVndavekG-GKILYGGKRDEGS-FFPPTVLENDTPD 354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569005993 341 EPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTlSSLPFGGV 418
Cdd:cd07145 355 MIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTRFRW-DNLPFGGF 431
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
116-418 |
1.78e-50 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 177.37 E-value: 1.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 116 EPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEETGQLL-EHK 193
Cdd:cd07093 116 QPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAgLPPGVVNVVHGFGPEAGAALvAHP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 194 -FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQEQ 272
Cdd:cd07093 196 dVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 273 LVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLLGCGR-----VAIGGQSDEGER-----YIAPTVLVDVQETE 341
Cdd:cd07093 276 FLERFVERAKALkVGDPLDPDTEVGPLISKEHLEKVLGYVELARaegatILTGGGRPELPDleggyFVEPTVITGLDNDS 355
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569005993 342 PVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDgFMYMTLsSLPFGGV 418
Cdd:cd07093 356 RVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNC-WLVRDL-RTPFGGV 430
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
106-418 |
4.44e-50 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 175.98 E-value: 4.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 106 TKLSTAFirKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPE 184
Cdd:cd07150 110 GTVSMSV--RRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 185 ETGQLL--EHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 262
Cdd:cd07150 188 EVGDELvdDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASR 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 263 ILCSQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLL------GcGRVAIGGQSDeGERYiAPTVLV 335
Cdd:cd07150 268 IIVEEPVYDEFVKKFVARASKLkVGDPRDPDTVIGPLISPRQVERIKRQVedavakG-AKLLTGGKYD-GNFY-QPTVLT 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 336 DVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQvLARTSSGGFCGNDGFMYMTLSSLPF 415
Cdd:cd07150 345 DVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFK-LAERLESGMVHINDPTILDEAHVPF 423
|
...
gi 569005993 416 GGV 418
Cdd:cd07150 424 GGV 426
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
109-420 |
7.67e-50 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 175.07 E-value: 7.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 109 STAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEE-- 185
Cdd:cd07105 90 TLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAgLPKGVLNVVTHSPEDap 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 186 --TGQLLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 262
Cdd:cd07105 170 evVEALIAHPaVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTER 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 263 ILCSQEMQEQLVPALQNAITRFYGDNPQtspnLGRIINQKHFKRLQGL----LGCG-RVAIGGQSDEGER--YIAPTVLV 335
Cdd:cd07105 250 IIVHESIADEFVEKLKAAAEKLFAGPVV----LGSLVSAAAADRVKELvddaLSKGaKLVVGGLADESPSgtSMPPTILD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 336 DVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGfCGNDGfmyMTL---SS 412
Cdd:cd07105 326 NVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA-VHING---MTVhdePT 401
|
....*...
gi 569005993 413 LPFGGVAS 420
Cdd:cd07105 402 LPHGGVKS 409
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
99-434 |
1.26e-49 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 174.93 E-value: 1.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 99 PVSTNLLTklstaFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFA 177
Cdd:cd07115 104 PVRGPFLN-----YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 178 VMLGGPEETGQ-LLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQ 255
Cdd:cd07115 179 VVTGFGEVAGAaLVEHPdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQ 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 256 TCVAPDYILCSQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLLGCG-----RVAIGGQSDeGER-- 327
Cdd:cd07115 259 MCTAGSRLLVHESIYDEFLERFTSLARSLrPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGreegaRLLTGGKRP-GARgf 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 328 YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNdgfMY 407
Cdd:cd07115 338 FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN---TY 414
|
330 340 350
....*....|....*....|....*....|..
gi 569005993 408 MTLSS-LPFGGVASP----EHSDAQRSPYSLP 434
Cdd:cd07115 415 NRFDPgSPFGGYKQSgfgrEMGREALDEYTEV 446
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
18-418 |
1.95e-49 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 173.80 E-value: 1.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 18 EEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESdMSEIILCENEVDLALKNLQTWMKD 97
Cdd:cd07100 2 EAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 98 EPVSTnlltKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCF 176
Cdd:cd07100 81 EPIET----DAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAgFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 177 AVMLGGPEETGQLLEHkfDYI---FFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA 253
Cdd:cd07100 157 QNLLIDSDQVEAIIAD--PRVrgvTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 254 GQTCVAPDYILCSQEMQEQLVPALQNAITRF-YGD--NPQTspNLGRIINQKHFKRLQGLL------GCgRVAIGGQSDE 324
Cdd:cd07100 235 GQSCIAAKRFIVHEDVYDEFLEKFVEAMAALkVGDpmDEDT--DLGPLARKDLRDELHEQVeeavaaGA-TLLLGGKRPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 325 GER-YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGND 403
Cdd:cd07100 312 GPGaFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFING 391
|
410
....*....|....*..
gi 569005993 404 gfmyMTLSS--LPFGGV 418
Cdd:cd07100 392 ----MVKSDprLPFGGV 404
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
25-417 |
2.74e-49 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 174.81 E-value: 2.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 25 KEAFNTG--KTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFES--DMSEIILC-ENEVDLALKnlqtwMKDE- 98
Cdd:cd07119 45 RRAFDSGewPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESeiDIDDVANCfRYYAGLATK-----ETGEv 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 99 -PVSTNLLTKlstafIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCF 176
Cdd:cd07119 120 yDVPPHVISR-----TVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 177 AVMLGGPEETGQ-LLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAG 254
Cdd:cd07119 195 NLVTGSGATVGAeLAESPdVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 255 QTCVAPDYILCSQEMQEQLVPAL---QNAITRFYGDNPQTspNLGRIINQKHFKRLQGLLGCG-----RVAIGGQSDEGE 326
Cdd:cd07119 275 QVCSAGSRLLVEESIHDKFVAALaerAKKIKLGNGLDADT--EMGPLVSAEHREKVLSYIQLGkeegaRLVCGGKRPTGD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 327 R-----YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCG 401
Cdd:cd07119 353 ElakgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWI 432
|
410
....*....|....*.
gi 569005993 402 NDgfMYMTLSSLPFGG 417
Cdd:cd07119 433 ND--YHPYFAEAPWGG 446
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
110-417 |
5.50e-49 |
|
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.
Pssm-ID: 132417 Cd Length: 472 Bit Score: 173.65 E-value: 5.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 110 TAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPEETGQL 189
Cdd:TIGR03374 130 TSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVVNILFGRGKTVGDP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 190 L--EHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQ 267
Cdd:TIGR03374 210 LtgHEKVRMVSLTGSIATGEHILSHTAPSIKRTHMELGGKAPVIVFDDADIDAVVEGVRTFGFYNAGQDCTAACRIYAQR 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 268 EMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGL------LGCGRVAIGGQSDEGE-RYIAPTVLVDVQE 339
Cdd:TIGR03374 290 GIYDTLVEKLGAAVATLkSGAPDDESTELGPLSSLAHLERVMKAveeakaLGHIKVITGGEKRKGNgYYFAPTLLAGAKQ 369
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569005993 340 TEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYmtLSSLPFGG 417
Cdd:TIGR03374 370 DDAIVQKEVFGPVVSITSFDDEEQVVNWANDSQYGLASSVWTKDVGRAHRLSARLQYGCTWVNTHFML--VSEMPHGG 445
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
110-418 |
1.45e-48 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 172.01 E-value: 1.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 110 TAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQ-YLDQSCFAVMLGGPEETG- 187
Cdd:cd07149 116 IGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEaGLPKGALNVVTGSGETVGd 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 188 QLLEHK-FDYIFFTGSPRVGKIVMTAAAkhLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCS 266
Cdd:cd07149 196 ALVTDPrVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVH 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 267 QEMQEQLVPALQNAITRF-YGD--NPQTspNLGRIINQKHFKRLQGLL-----GCGRVAIGGQSDEgeRYIAPTVLVDVQ 338
Cdd:cd07149 274 EDIYDEFLERFVAATKKLvVGDplDEDT--DVGPMISEAEAERIEEWVeeaveGGARLLTGGKRDG--AILEPTVLTDVP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 339 ETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYmTLSSLPFGGV 418
Cdd:cd07149 350 PDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSSTF-RVDHMPYGGV 428
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
111-418 |
2.72e-48 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 172.01 E-value: 2.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 111 AFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLG-GPEETGQ 188
Cdd:cd07091 135 AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGfGPTAGAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 189 LLEH-KFDYIFFTGSPRVGKIVMTAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANrVAWFR-YFNAGQTCVAPDYILC 265
Cdd:cd07091 215 ISSHmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVE-WAAFGiFFNQGQCCCAGSRIFV 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 266 SQEMQEQLVPAL-QNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCG-----RVAIGGQ--SDEGeRYIAPTVLVDV 337
Cdd:cd07091 294 QESIYDEFVEKFkARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGkkegaTLLTGGErhGSKG-YFIQPTVFTDV 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 338 QETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGF---CGNDgfmymTLSSLP 414
Cdd:cd07091 373 KDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVwvnTYNV-----FDAAVP 447
|
....
gi 569005993 415 FGGV 418
Cdd:cd07091 448 FGGF 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
13-418 |
5.99e-48 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 171.41 E-value: 5.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 13 GTDPFEEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESdmseiilcENEVDLALKNLQ 92
Cdd:PLN02278 60 GRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEA--------IGEVAYGASFLE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 93 tWMKDEPVSTN---LLTKLSTA--FIRKEPFGLVLIIAPWNYPVNlMIIPLVG-AIAAGNCVVLKPSEISKNTEKVLAEL 166
Cdd:PLN02278 132 -YFAEEAKRVYgdiIPSPFPDRrlLVLKQPVGVVGAITPWNFPLA-MITRKVGpALAAGCTVVVKPSELTPLTALAAAEL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 167 LPQY-LDQSCFAVMLGGPEETGQLL--EHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVAN 243
Cdd:PLN02278 210 ALQAgIPPGVLNVVMGDAPEIGDALlaSPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 244 RVAWFRYFNAGQTCVAPDYILCSQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQG------------L 310
Cdd:PLN02278 290 GALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVEShvqdavskgakvL 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 311 LGCGRVAIGGQsdegerYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQV 390
Cdd:PLN02278 370 LGGKRHSLGGT------FYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRV 443
|
410 420
....*....|....*....|....*...
gi 569005993 391 LARTSSGGFCGNDGFmyMTLSSLPFGGV 418
Cdd:PLN02278 444 SEALEYGIVGVNEGL--ISTEVAPFGGV 469
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
39-420 |
7.00e-48 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 170.17 E-value: 7.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 39 RAEQLQSLGRFLQDNSKQLHDAL----DGDLGKSGFESDMSeIILCENEVDLALKNLQTWMKDEPvstnllTKLSTAfiR 114
Cdd:cd07152 37 RAAVLRRAADLLEEHADEIADWIvresGSIRPKAGFEVGAA-IGELHEAAGLPTQPQGEILPSAP------GRLSLA--R 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 115 KEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKP---SEISKNTekVLAELLPQY-LDQSCFAVMLGGPEETGQLL 190
Cdd:cd07152 108 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPdprTPVSGGV--VIARLFEEAgLPAGVLHVLPGGADAGEALV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 191 EH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEM 269
Cdd:cd07152 186 EDpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 270 QEQLVPALQNAITRFYGDNPQTSP-NLGRIINQKHFKRLQGL------LGcGRVAIGGQSDegERYIAPTVLVDVQETEP 342
Cdd:cd07152 266 ADAYTAKLAAKAKHLPVGDPATGQvALGPLINARQLDRVHAIvddsvaAG-ARLEAGGTYD--GLFYRPTVLSGVKPGMP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 343 VMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGfmymTLSS---LPFGGVA 419
Cdd:cd07152 343 AFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ----TVNDephNPFGGMG 418
|
.
gi 569005993 420 S 420
Cdd:cd07152 419 A 419
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
109-417 |
1.44e-47 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 169.61 E-value: 1.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 109 STAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEETG 187
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 188 QLL-EHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILC 265
Cdd:TIGR01804 205 PLLvNHPdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 266 SQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLLGCG-----RVAIGGQSDEGER-----YIAPTVL 334
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIEKGkaegaTLATGGGRPENVGlqngfFVEPTVF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 335 VDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDgfMYMTLSSLP 414
Cdd:TIGR01804 365 ADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYPAEAP 442
|
...
gi 569005993 415 FGG 417
Cdd:TIGR01804 443 FGG 445
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
111-418 |
1.64e-47 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 169.08 E-value: 1.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 111 AFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEETGQL 189
Cdd:cd07146 114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEIGDE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 190 LEH--KFDYIFFTGSPRVGKIVmtAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQ 267
Cdd:cd07146 194 LIThpDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 268 EMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGL----LGCG-RVAIGGQSDeGERYiAPTVLVDVQETE 341
Cdd:cd07146 272 SVADEFVDLLVEKSAALvVGDPMDPATDMGTVIDEEAAIQIENRveeaIAQGaRVLLGNQRQ-GALY-APTVLDHVPPDA 349
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569005993 342 PVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLSSlPFGGV 418
Cdd:cd07146 350 ELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSELS-PFGGV 425
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
5-390 |
4.69e-47 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 169.33 E-value: 4.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 5 GKHPRADQgtDPFEEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFES--DMSEII-LCE 81
Cdd:cd07124 61 GTVQKATK--EEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEAdaDVAEAIdFLE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 82 NEVDLALKNLQTWMKDEPVSTNLLtklstafiRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEK 161
Cdd:cd07124 139 YYAREMLRLRGFPVEMVPGEDNRY--------VYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 162 VLAELLPQY-LDQSCFAVMLGGPEETGQ-LLEH-KFDYIFFTGSPRVGKIVMTAAAK------HLTPITLELGGKNPCYV 232
Cdd:cd07124 211 KLVEILEEAgLPPGVVNFLPGPGEEVGDyLVEHpDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 233 DDNCDPQTVANRV--AWFRYfnAGQTCVApdyilCS-----QEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHF 304
Cdd:cd07124 291 DEDADLDEAAEGIvrSAFGF--QGQKCSA-----CSrvivhESVYDEFLERLVERTKALkVGDPEDPEVYMGPVIDKGAR 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 305 KRLQGLL----GCGRVAIGGQSDEGER---YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLAL 377
Cdd:cd07124 364 DRIRRYIeigkSEGRLLLGGEVLELAAegyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTG 443
|
410
....*....|...
gi 569005993 378 YAYSNNAEVIKQV 390
Cdd:cd07124 444 GVFSRSPEHLERA 456
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
112-386 |
1.04e-46 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 166.06 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 112 FIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEETGQLL 190
Cdd:PRK10090 66 LLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 191 --EHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQE 268
Cdd:PRK10090 146 agNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 269 MQEQLVPALQNAITRFYGDNP--QTSPNLGRIINQKHFKRLQGLLG-----CGRVAIGGQSDEGERYI-APTVLVDVQET 340
Cdd:PRK10090 226 IYDQFVNRLGEAMQAVQFGNPaeRNDIAMGPLINAAALERVEQKVAraveeGARVALGGKAVEGKGYYyPPTLLLDVRQE 305
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 569005993 341 EPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEV 386
Cdd:PRK10090 306 MSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNV 351
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
111-418 |
1.21e-46 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 167.58 E-value: 1.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 111 AFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEETGQ- 188
Cdd:cd07144 138 AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSa 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 189 LLEH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQ 267
Cdd:cd07144 218 LAEHpDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 268 EMQEQLVPALQNAITRFY--GDNPQTSPNLGRIINQKHFKRLQGLLGCGR------VAIGGQSDEGER---YIAPTVLVD 336
Cdd:cd07144 298 SIYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKkegaklVYGGEKAPEGLGkgyFIPPTIFTD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 337 VQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGF---CGNDGFMYMtlssl 413
Cdd:cd07144 378 VPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVwinSSNDSDVGV----- 452
|
....*
gi 569005993 414 PFGGV 418
Cdd:cd07144 453 PFGGF 457
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
108-418 |
1.89e-46 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 166.60 E-value: 1.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 108 LSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEET 186
Cdd:cd07139 128 GGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPADREVG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 187 GQLLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILC 265
Cdd:cd07139 208 EYLVRHPgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 266 SQEMQEQLVPALQNAITRF-YGD--NPQTSpnLGRIINQKHFKRLQGLLGCG-----RVAIGGQSDEG-ER--YIAPTVL 334
Cdd:cd07139 288 PRSRYDEVVEALAAAVAALkVGDplDPATQ--IGPLASARQRERVEGYIAKGraegaRLVTGGGRPAGlDRgwFVEPTLF 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 335 VDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNdgfMYMTLSSLP 414
Cdd:cd07139 366 ADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN---GFRLDFGAP 442
|
....
gi 569005993 415 FGGV 418
Cdd:cd07139 443 FGGF 446
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
18-376 |
4.02e-46 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 165.98 E-value: 4.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 18 EEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIilcenevDLALKNLQTW--- 94
Cdd:cd07559 41 DLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLAADI-------PLAIDHFRYFagv 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 95 MKDEPVSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQS 174
Cdd:cd07559 114 IRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 175 CFAVMLGGPEETGQ-LLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNP-------CYVDDNCDPQTVANRV 245
Cdd:cd07559 194 VVNVVTGFGSEAGKpLASHPrIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPniffddaMDADDDFDDKAEEGQL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 246 AWFryFNAGQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQ-TSPNLGRIINQKHFKRLQGLLGCGR-----VAIG 319
Cdd:cd07559 274 GFA--FNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLdPETMMGAQVSKDQLEKILSYVDIGKeegaeVLTG 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569005993 320 GQ-----SDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLA 376
Cdd:cd07559 352 GErltlgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLG 413
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
111-418 |
5.83e-46 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 165.30 E-value: 5.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 111 AFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELL-PQYLDQSCFAVMLGGPEETGQL 189
Cdd:cd07094 117 AWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAGVPEGVLQVVTGEREVLGDA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 190 L--EHKFDYIFFTGSPRVGKIVMTAAAKhlTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQ 267
Cdd:cd07094 197 FaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 268 EMQEQLVPALQNAITRFYGDNP-QTSPNLGRIINQKHFKRLQ-----GLLGCGRVAIGGQSDegERYIAPTVLVDVQETE 341
Cdd:cd07094 275 ELYDEFIEAFVAAVKKLKVGDPlDEDTDVGPLISEEAAERVErwveeAVEAGARLLCGGERD--GALFKPTVLEDVPRDT 352
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569005993 342 PVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTlSSLPFGGV 418
Cdd:cd07094 353 KLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRT-DWMPFGGV 428
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
111-369 |
1.37e-45 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 164.26 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 111 AFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAEL-----LPQYLdqscFAVMLGGPEE 185
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagFPPGV----VNVVTGFGPE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 186 TGQLL-EH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYI 263
Cdd:cd07114 189 TGEALvEHpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 264 LCSQEMQEQLVPALQnAITRF--YGD--NPQTspNLGRIINQKHFKRLQGLLGC-----GRVAIGGQSDEGER-----YI 329
Cdd:cd07114 269 LVQRSIYDEFVERLV-ARARAirVGDplDPET--QMGPLATERQLEKVERYVARareegARVLTGGERPSGADlgagyFF 345
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 569005993 330 APTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMN 369
Cdd:cd07114 346 EPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALAN 385
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
25-376 |
2.90e-45 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 163.78 E-value: 2.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 25 KEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEvdlaLKNLQTWMKDEPVSTNL 104
Cdd:cd07117 48 QEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAVDIPLAADH----FRYFAGVIRAEEGSANM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 105 LTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPE 184
Cdd:cd07117 124 IDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 185 ETGQ-LLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 262
Cdd:cd07117 204 KSGEyLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 263 ILCSQEMQEQLVPALQNAITRFYGDNPQT-SPNLGRIINQKHFKRLQGLLGCG-----RVAIGGQS------DEGErYIA 330
Cdd:cd07117 284 IFVQEGIYDEFVAKLKEKFENVKVGNPLDpDTQMGAQVNKDQLDKILSYVDIAkeegaKILTGGHRltenglDKGF-FIE 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 569005993 331 PTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLA 376
Cdd:cd07117 363 PTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLG 408
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
25-397 |
3.26e-45 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 164.14 E-value: 3.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 25 KEAFNTGKTK-----TAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFES--DMSEIILC-ENEVDLA--LKNLQTw 94
Cdd:PLN02467 55 RKAFKRNKGKdwartTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAawDMDDVAGCfEYYADLAeaLDAKQK- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 95 mkdEPVSTNLLTKLStaFIRKEPFGLVLIIAPWNYPVnLMIIPLVG-AIAAGNCVVLKPSEISKNTEKVLAELLPQY-LD 172
Cdd:PLN02467 134 ---APVSLPMETFKG--YVLKEPLGVVGLITPWNYPL-LMATWKVApALAAGCTAVLKPSELASVTCLELADICREVgLP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 173 QSCFAVMLG-GPEETGQLLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDpqtVANRVAW--F 248
Cdd:PLN02467 208 PGVLNVVTGlGTEAGAPLASHPgVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVD---LDKAVEWamF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 249 RYF-NAGQTCVAPDYILCSQ----EMQEQLVPALQNaITrfYGDNPQTSPNLGRIINQKHFKRLQGLLGCGR-----VAI 318
Cdd:PLN02467 285 GCFwTNGQICSATSRLLVHEriasEFLEKLVKWAKN-IK--ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKsegatILC 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 319 GGQSDEGER---YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTS 395
Cdd:PLN02467 362 GGKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQ 441
|
..
gi 569005993 396 SG 397
Cdd:PLN02467 442 AG 443
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
25-420 |
3.72e-45 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 162.93 E-value: 3.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 25 KEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLH--DALDGdlgksGFEsdMSEIIlceNEVDLALK------NLQTWMK 96
Cdd:cd07107 29 RAAFPEWRATTPLERARMLRELATRLREHAEELAliDALDC-----GNP--VSAML---GDVMVAAAlldyfaGLVTELK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 97 DE--PVSTNLLTklstaFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQS 174
Cdd:cd07107 99 GEtiPVGGRNLH-----YTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 175 CFAVMLGGPEETGQ-LLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANR-VAWFRYF 251
Cdd:cd07107 174 VFNILPGDGATAGAaLVRHPdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAaVAGMNFT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 252 NAGQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPqTSPN--LGRIINQKHFKRLQGLLGCG-----RVAIGGQSDE 324
Cdd:cd07107 254 WCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDP-TDPAttMGPLVSRQQYDRVMHYIDSAkregaRLVTGGGRPE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 325 GER-----YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNaevIKQVL--ARTSSG 397
Cdd:cd07107 333 GPAleggfYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTND---ISQAHrtARRVEA 409
|
410 420
....*....|....*....|...
gi 569005993 398 GFCGNDGFMYMTLsSLPFGGVAS 420
Cdd:cd07107 410 GYVWINGSSRHFL-GAPFGGVKN 431
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
110-418 |
7.93e-45 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 162.61 E-value: 7.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 110 TAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEETGQ 188
Cdd:cd07113 135 TAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNGKGAVGAQ 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 189 LLEH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQ 267
Cdd:cd07113 215 LISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 268 EMQEQLVPALQNAITRFY-GDNPQTSPNLGRIINQKHFKRLQGLLGCGR-----VAIGGQSDEGERY-IAPTVLVDVQET 340
Cdd:cd07113 295 SKFDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLDDARaegdeIVRGGEALAGEGYfVQPTLVLARSAD 374
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569005993 341 EPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNdgfMYMTLS-SLPFGGV 418
Cdd:cd07113 375 SRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLDpAVPFGGM 450
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
108-418 |
3.11e-44 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 160.55 E-value: 3.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 108 LSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEET 186
Cdd:cd07101 109 LTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAgLPRDLWQVVTGPGSEV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 187 GQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVAnRVAWFRYF-NAGQTCVAPDYILC 265
Cdd:cd07101 189 GGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAA-AGAVRACFsNAGQLCVSIERIYV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 266 SQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLLGCGR-----VAIGGQS--DEGERYIAPTVLVDV 337
Cdd:cd07101 268 HESVYDEFVRRFVARTRALrLGAALDYGPDMGSLISQAQLDRVTAHVDDAVakgatVLAGGRArpDLGPYFYEPTVLTGV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 338 QETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFM--YMTLSSlPF 415
Cdd:cd07101 348 TEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAaaWASIDA-PM 426
|
...
gi 569005993 416 GGV 418
Cdd:cd07101 427 GGM 429
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
116-389 |
8.41e-44 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 160.49 E-value: 8.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 116 EPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEETGQ-LLEH- 192
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDyLVDHp 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 193 KFDYIFFTGSPRVGKIVMTAAAK------HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVApdyilCS 266
Cdd:PRK03137 250 KTRFITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSA-----CS 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 267 Q---------EMQEQLVpALQNAITrfYGdNPQTSPNLGRIINQKHFKRLQGLL----GCGRVAIGGQSDEGERY-IAPT 332
Cdd:PRK03137 325 RaivhedvydEVLEKVV-ELTKELT--VG-NPEDNAYMGPVINQASFDKIMSYIeigkEEGRLVLGGEGDDSKGYfIQPT 400
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 569005993 333 VLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQ 389
Cdd:PRK03137 401 IFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEK 457
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
112-372 |
2.38e-43 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 158.57 E-value: 2.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 112 FIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEETGQ-L 189
Cdd:cd07097 130 ETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGSGSEVGQaL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 190 LEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQE 268
Cdd:cd07097 210 VEHPdVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 269 MQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRL-----QGLLGCGRVAIGGQSDEGER---YIAPTVLVDVQE 339
Cdd:cd07097 290 IHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDlryieIARSEGAKLVYGGERLKRPDegyYLAPALFAGVTN 369
|
250 260 270
....*....|....*....|....*....|...
gi 569005993 340 TEPVMQEEIFGPILPLVTVRSLDEAIEFMNQRE 372
Cdd:cd07097 370 DMRIAREEIFGPVAAVIRVRDYDEALAIANDTE 402
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
18-444 |
5.31e-42 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 155.41 E-value: 5.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 18 EEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESD--MSEII-LCE----NEVDLALKN 90
Cdd:TIGR01237 72 EHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADaeVAEAIdFMEyyarQMIELAKGK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 91 LQTWMKDEpvsTNLLTKlstafirkEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY 170
Cdd:TIGR01237 152 PVNSREGE---TNQYVY--------TPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 171 -LDQSCFAVMLGGPEETGQ-LLEH-KFDYIFFTGSPRVGKIVMTAAAK------HLTPITLELGGKNPCYVDDNCDPQTV 241
Cdd:TIGR01237 221 gLPKGVVQFVPGSGSEVGDyLVDHpKTSLITFTGSREVGTRIFERAAKvqpgqkHLKRVIAEMGGKDTVIVDEDADIELA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 242 ANRVAWFRYFNAGQTCVAPDYILCSQEMQEQLVPA-LQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCG----RV 316
Cdd:TIGR01237 301 AQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERfVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGkaegRL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 317 AIGGQSDEGERY-IAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTS 395
Cdd:TIGR01237 381 VSGGCGDDSKGYfIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFE 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 569005993 396 SGGFCGNDGFMYMTLSSLPFGGV-ASPEHSDAQRSPYSLPFRFPRAVPRR 444
Cdd:TIGR01237 461 VGNLYFNRNITGAIVGYQPFGGFkMSGTDSKAGGPDYLALFMQAKTVTEM 510
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
106-372 |
5.71e-42 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 154.65 E-value: 5.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 106 TKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSeisknTEKVL-AELLPQYLDQSCF-----AVM 179
Cdd:cd07082 130 TKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPA-----TQGVLlGIPLAEAFHDAGFpkgvvNVV 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 180 LG-GPEETGQLLEH-KFDYIFFTGSPRVGKIVMTAAAKhlTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTC 257
Cdd:cd07082 205 TGrGREIGDPLVTHgRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRC 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 258 VAPDYILCSQEMQEQLVPALQNAITRFYGDNP-QTSPNLGRIINQKHFKRLQGLL------GcGRVAIGGQSdEGERYIA 330
Cdd:cd07082 283 TAIKRVLVHESVADELVELLKEEVAKLKVGMPwDNGVDITPLIDPKSADFVEGLIddavakG-ATVLNGGGR-EGGNLIY 360
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 569005993 331 PTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQRE 372
Cdd:cd07082 361 PTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSN 402
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
111-417 |
1.81e-41 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 153.45 E-value: 1.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 111 AFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEETGQL 189
Cdd:cd07143 138 TYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 190 LE-H-KFDYIFFTGSPRVGKIVMTAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCS 266
Cdd:cd07143 218 ISsHmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 267 QEMQEQLVPALQNAITRFYGDNPqTSPNL--GRIINQKHFKRLQGLLGCGR-----VAIGGQSDEGERY-IAPTVLVDVQ 338
Cdd:cd07143 298 EGIYDKFVKRFKEKAKKLKVGDP-FAEDTfqGPQVSQIQYERIMSYIESGKaegatVETGGKRHGNEGYfIEPTIFTDVT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 339 ETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDgfmYMTLS-SLPFGG 417
Cdd:cd07143 377 EDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNC---YNLLHhQVPFGG 453
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
37-369 |
5.15e-41 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 152.29 E-value: 5.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 37 KFRA---EQLQSLGRFL-QDNSKQLHDALdGDLGKsGFESdmseiilceneVDLALkNLQTWMKDEpVSTNLLTKLSTAF 112
Cdd:cd07085 68 KFRQlleENLDELARLItLEHGKTLADAR-GDVLR-GLEV-----------VEFAC-SIPHLLKGE-YLENVARGIDTYS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 113 IRkEPFGLVLIIAPWNYP--VNLMIIPLvgAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEETGQL 189
Cdd:cd07085 133 YR-QPLGVVAGITPFNFPamIPLWMFPM--AIACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHGGKEAVNAL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 190 LEH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQE 268
Cdd:cd07085 210 LDHpDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGD 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 269 MQEQLVPALQNAITRF---YGDNPQTspNLGRIINQKHFKRLQGLLGCG-----RVAIGG---QSDEGER--YIAPTVLV 335
Cdd:cd07085 290 EADEWIPKLVERAKKLkvgAGDDPGA--DMGPVISPAAKERIEGLIESGveegaKLVLDGrgvKVPGYENgnFVGPTILD 367
|
330 340 350
....*....|....*....|....*....|....
gi 569005993 336 DVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMN 369
Cdd:cd07085 368 NVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIIN 401
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
117-370 |
1.15e-40 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 151.18 E-value: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 117 PFGLVLIIAPWNYPV-----NLMIiplvgAIAAGNCVVLKPSE----ISKNTEKVLAELLPQY-LDQSCFAVMLGGpEET 186
Cdd:cd07086 133 PLGVVGVITAFNFPVavpgwNAAI-----ALVCGNTVVWKPSEttplTAIAVTKILAEVLEKNgLPPGVVNLVTGG-GDG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 187 GQLLEH--KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYIL 264
Cdd:cd07086 207 GELLVHdpRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLI 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 265 CSQEMQEQLVPALQNAITRFYGDNPQTSPNL-GRIINQKHFKRLQGLL------GcGRVAIGG---QSDEGERYIAPTVL 334
Cdd:cd07086 287 VHESVYDEFLERLVKAYKQVRIGDPLDEGTLvGPLINQAAVEKYLNAIeiaksqG-GTVLTGGkriDGGEPGNYVEPTIV 365
|
250 260 270
....*....|....*....|....*....|....*.
gi 569005993 335 VDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQ 370
Cdd:cd07086 366 TGVTDDARIVQEETFAPILYVIKFDSLEEAIAINND 401
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
10-376 |
1.27e-40 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 150.57 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 10 ADQGTDPFEEKLQRLKEAF-NTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESdMSEIILCENEVD--- 85
Cdd:cd07120 14 ADGGVAEAEAAIAAARRAFdETDWAHDPRLRARVLLELADAFEANAERLARLLALENGKILGEA-RFEISGAISELRyya 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 86 -LALKNLQTWMKDEPvstnllTKLSTafIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLA 164
Cdd:cd07120 93 gLARTEAGRMIEPEP------GSFSL--VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAII 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 165 ELLPQ--YLDQSCFAVMLGGPEETGQLL--EHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQT 240
Cdd:cd07120 165 RILAEipSLPAGVVNLFTESGSEGAAHLvaSPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 241 VANRVAWFRYFNAGQTCVAPDYILC----SQEMQEQLVPALQNAITrfyGDNPQTSPNLGRIINQKHFKRLQGLLG---- 312
Cdd:cd07120 245 ALPKLERALTIFAGQFCMAGSRVLVqrsiADEVRDRLAARLAAVKV---GPGLDPASDMGPLIDRANVDRVDRMVEraia 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569005993 313 -CGRVAI-GGQSDEGER---YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLA 376
Cdd:cd07120 322 aGAEVVLrGGPVTEGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLA 390
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
108-418 |
1.59e-40 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 151.57 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 108 LSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEET 186
Cdd:PRK09407 145 LTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVVTGPGPVV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 187 GQ-LLEHKfDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILC 265
Cdd:PRK09407 225 GTaLVDNA-DYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYV 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 266 SQEMQEQLVPALQNAITRF-----YGDNPQtspnLGRIINQKHFKRLQGLLGCGR-----VAIGGQS--DEGERYIAPTV 333
Cdd:PRK09407 304 HESIYDEFVRAFVAAVRAMrlgagYDYSAD----MGSLISEAQLETVSAHVDDAVakgatVLAGGKArpDLGPLFYEPTV 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 334 LVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGF--MYMTLS 411
Cdd:PRK09407 380 LTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYaaAWGSVD 459
|
....*..
gi 569005993 412 SlPFGGV 418
Cdd:PRK09407 460 A-PMGGM 465
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
111-383 |
4.38e-40 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 149.81 E-value: 4.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 111 AFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAEL-------------LPQYldqscfa 177
Cdd:cd07141 139 TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLikeagfppgvvnvVPGY------- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 178 vmlgGPEETGQLLEH-KFDYIFFTGSPRVGKIVMTAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQ 255
Cdd:cd07141 212 ----GPTAGAAISSHpDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 256 TCVAPDYILCSQEMQEQLVP-ALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCG-----RVAIGGqSDEGER-- 327
Cdd:cd07141 288 CCCAGSRTFVQESIYDEFVKrSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGkkegaKLECGG-KRHGDKgy 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 569005993 328 YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNN 383
Cdd:cd07141 367 FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKD 422
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
18-417 |
7.72e-40 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 149.27 E-value: 7.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 18 EEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFES--DMSEII-LCENEVDLALKnlqtW 94
Cdd:cd07083 58 EAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAidDVAEAIdFIRYYARAALR----L 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 95 MKDEPVSTNLLTKLSTAFIRkePFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSE----ISKNTEKVLAEL-LPQ 169
Cdd:cd07083 134 RYPAVEVVPYPGEDNESFYV--GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEdavvVGYKVFEIFHEAgFPP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 170 YLDQSCFAVmlgGPEETGQLLEH-KFDYIFFTGSPRVGKIVMTAAAKHLT------PITLELGGKNPCYVDDNCDPQTVA 242
Cdd:cd07083 212 GVVQFLPGV---GEEVGAYLTEHeRIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 243 NRVAWFRYFNAGQTCVAPDYILCSQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLLGCGR----VA 317
Cdd:cd07083 289 EGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLsVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKnegqLV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 318 IGGQSDEGERY-IAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLD--EAIEFMNQREKPLALYAYSNNAEVIKQVLART 394
Cdd:cd07083 369 LGGKRLEGEGYfVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREF 448
|
410 420
....*....|....*....|...
gi 569005993 395 SSGGFCGNDGFMYMTLSSLPFGG 417
Cdd:cd07083 449 HVGNLYINRKITGALVGVQPFGG 471
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
25-417 |
2.41e-39 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 147.54 E-value: 2.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 25 KEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLH--DALDGdlGKSGFES-DMseiilcenEVDLALKNLQ---TWMKde 98
Cdd:cd07111 69 RTAFESWSALPGHVRARHLYRIARHIQKHQRLFAvlESLDN--GKPIRESrDC--------DIPLVARHFYhhaGWAQ-- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 99 pvstnlltKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFA 177
Cdd:cd07111 137 --------LLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 178 VMLGGPEETGQLLEH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQT 256
Cdd:cd07111 209 IVTGNGSFGSALANHpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 257 CVAPDYILCSQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLLGCGRvAIGGQ--------SDEGER 327
Cdd:cd07111 289 CCAGSRLLVQESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR-AEGADvfqpgadlPSKGPF 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 328 YiAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMY 407
Cdd:cd07111 368 Y-PPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLF 446
|
410
....*....|
gi 569005993 408 MtlSSLPFGG 417
Cdd:cd07111 447 D--AAAGFGG 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
109-417 |
3.84e-38 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 143.98 E-value: 3.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 109 STAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGpEETG 187
Cdd:cd07090 108 SFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETG 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 188 QLLEHKFDY--IFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTC------VA 259
Cdd:cd07090 187 QLLCEHPDVakVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCsngtrvFV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 260 PDYILcsQEMQEQLVPALQNAITrfyGDNPQTSPNLGRIINQKHFKRLQGLLGCG-----RVAIGGQSD------EGERY 328
Cdd:cd07090 267 QRSIK--DEFTERLVERTKKIRI---GDPLDEDTQMGALISEEHLEKVLGYIESAkqegaKVLCGGERVvpedglENGFY 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 329 IAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDgfmY- 407
Cdd:cd07090 342 VSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT---Yn 418
|
330
....*....|
gi 569005993 408 MTLSSLPFGG 417
Cdd:cd07090 419 ISPVEVPFGG 428
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
115-417 |
5.50e-38 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 143.79 E-value: 5.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 115 KEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLG-GPEETGQLLEH 192
Cdd:cd07142 139 HEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGfGPTAGAAIASH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 193 K-FDYIFFTGSPRVGKIVMTAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQ 270
Cdd:cd07142 219 MdVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIY 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 271 EQLVP-ALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCG-----RVAIGGQS--DEGeRYIAPTVLVDVQETEP 342
Cdd:cd07142 299 DEFVEkAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGkeegaTLITGGDRigSKG-YYIQPTIFSDVKDDMK 377
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569005993 343 VMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGN--DGFMymtlSSLPFGG 417
Cdd:cd07142 378 IARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDVFD----ASIPFGG 450
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
115-417 |
6.32e-38 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 144.19 E-value: 6.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 115 KEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLG-GPEETGQLLEH 192
Cdd:PLN02766 156 KEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGfGPTAGAAIASH 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 193 -KFDYIFFTGSPRVGKIVMTAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQ 270
Cdd:PLN02766 236 mDVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIY 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 271 EQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLLGCGR-----VAIGGQS--DEGeRYIAPTVLVDVQETEP 342
Cdd:PLN02766 316 DEFVKKLVEKAKDWvVGDPFDPRARQGPQVDKQQFEKILSYIEHGKregatLLTGGKPcgDKG-YYIEPTIFTDVTEDMK 394
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569005993 343 VMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMtlSSLPFGG 417
Cdd:PLN02766 395 IAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFD--PDCPFGG 467
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
113-417 |
1.12e-37 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 142.83 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 113 IRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSE---ISKNTekVLAELLPQY-LDQSCFAVMLGGPEETG- 187
Cdd:cd07151 126 VYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASdtpITGGL--LLAKIFEEAgLPKGVLNVVVGAGSEIGd 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 188 QLLEHKF-DYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCS 266
Cdd:cd07151 204 AFVEHPVpRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVH 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 267 QEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLL------GcGRVAIGGQSdEGeRYIAPTVLVDVQE 339
Cdd:cd07151 284 EDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDKIeqaveeG-ATLLVGGEA-EG-NVLEPTVLSDVTN 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 340 TEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDgfmyMTLSS---LPFG 416
Cdd:cd07151 361 DMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIND----QPVNDephVPFG 436
|
.
gi 569005993 417 G 417
Cdd:cd07151 437 G 437
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
111-418 |
1.25e-36 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 139.69 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 111 AFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELL-PQYLDQSCFAVMLGGPEETGQL 189
Cdd:cd07147 117 GLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLaETGLPKGAFSVLPCSRDDADLL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 190 LEHK-FDYIFFTGSPRVG-KIVMTAAAKHltpITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQ 267
Cdd:cd07147 197 VTDErIKLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 268 EMQEQ----LVPALQNAITrfyGDNPQTSPNLGRIINQKHFKRLQGLL-----GCGRVAIGGQSDEGerYIAPTVLVDVQ 338
Cdd:cd07147 274 SVYDEfksrLVARVKALKT---GDPKDDATDVGPMISESEAERVEGWVneavdAGAKLLTGGKRDGA--LLEPTILEDVP 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 339 ETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQ-----------REKPLALYAYsNNAEVikqvlartssGGFCGNDGFMY 407
Cdd:cd07147 349 PDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDskfglqagvftRDLEKALRAW-DELEV----------GGVVINDVPTF 417
|
330
....*....|.
gi 569005993 408 mTLSSLPFGGV 418
Cdd:cd07147 418 -RVDHMPYGGV 427
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
111-417 |
7.83e-36 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 138.11 E-value: 7.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 111 AFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLGGPEETGQL 189
Cdd:PRK09847 151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 190 L--EHKFDYIFFTGSPRVGKIVMT-AAAKHLTPITLELGGKNPCYVDDNC-DPQTVANRVAWFRYFNAGQTCVAPDYILC 265
Cdd:PRK09847 231 LsrHNDIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 266 SQEMQEQLVPALQNAITRFY-GD--NPQTSpnLGRIINQKHFKR----LQGLLGCGRVAIGGQSDEGERYIAPTVLVDVQ 338
Cdd:PRK09847 311 EESIADEFLALLKQQAQNWQpGHplDPATT--MGTLIDCAHADSvhsfIREGESKGQLLLDGRNAGLAAAIGPTIFVDVD 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 339 ETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGG-FCG--NDGFMymtlsSLPF 415
Cdd:PRK09847 389 PNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSvFVNnyNDGDM-----TVPF 463
|
..
gi 569005993 416 GG 417
Cdd:PRK09847 464 GG 465
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
25-418 |
3.17e-35 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 135.48 E-value: 3.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 25 KEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESdMSEIILCENEVDLALKNLQ--TWMKDEPvst 102
Cdd:cd07095 10 RAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA-QTEVAAMAGKIDISIKAYHerTGERATP--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 103 nllTKLSTAFIRKEPFGLVLIIAPWNYPVNL---MIIPlvgAIAAGNCVVLKPSEISKNTEKVLAELL-PQYLDQSCFAV 178
Cdd:cd07095 86 ---MAQGRAVLRHRPHGVMAVFGPFNFPGHLpngHIVP---ALLAGNTVVFKPSELTPAVAELMVELWeEAGLPPGVLNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 179 MLGGPEETGQLLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPI-TLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQT 256
Cdd:cd07095 160 VQGGRETGEALAAHEgIDGLLFTGSAATGLLLHRQFAGRPGKIlALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 257 CV-APDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPN-LGRIINQKHFKRL----QGLLGCGRVAIGGQS--DEGERY 328
Cdd:cd07095 240 CTcARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPfMGPLIIAAAAARYllaqQDLLALGGEPLLAMErlVAGTAF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 329 IAPTvLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGN---DGf 405
Cdd:cd07095 320 LSPG-IIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNrptTG- 397
|
410
....*....|...
gi 569005993 406 mymTLSSLPFGGV 418
Cdd:cd07095 398 ---ASSTAPFGGV 407
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
115-420 |
8.60e-35 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 135.03 E-value: 8.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 115 KEPFGLVLIIAPWNYPVnLMIIPLVG-AIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLG-----GPEETG 187
Cdd:PRK11241 144 KQPIGVTAAITPWNFPA-AMITRKAGpALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGsagavGGELTS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 188 QLLEHKFDyifFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQ 267
Cdd:PRK11241 223 NPLVRKLS---FTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 268 EMQEQLVPALQNAITRFY-GDNPQTSPNLGRIINQKHFKRLQ-----GLLGCGRVAIGGQSDE-GERYIAPTVLVDVQET 340
Cdd:PRK11241 300 GVYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTILVDVPAN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 341 EPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLSslPFGGVAS 420
Cdd:PRK11241 380 AKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKA 457
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
116-417 |
3.72e-32 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 128.39 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 116 EPFGLVLIIAPWNYPVnLMIIPLVG-AIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVMLG-GPEETGQLLEH 192
Cdd:PLN02466 194 EPIGVAGQIIPWNFPL-LMFAWKVGpALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGfGPTAGAALASH 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 193 -KFDYIFFTGSPRVGKIVMTAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQ 270
Cdd:PLN02466 273 mDVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVY 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 271 EQLV-PALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCG-----RVAIGGQ--SDEGeRYIAPTVLVDVQETEP 342
Cdd:PLN02466 353 DEFVeKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGvesgaTLECGGDrfGSKG-YYIQPTVFSNVQDDML 431
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569005993 343 VMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIkQVLARTSSGGFCGNDGFMYMTlSSLPFGG 417
Cdd:PLN02466 432 IAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTA-NTLSRALRVGTVWVNCFDVFD-AAIPFGG 504
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
111-393 |
8.55e-31 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 123.84 E-value: 8.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 111 AFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-LDQSCFAVmLGGPEETGQL 189
Cdd:PRK13252 136 VYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNV-VQGDGRVGAW 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 190 L-EH-KFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQT------VANrvawfrYFNAGQTCVAPD 261
Cdd:PRK13252 215 LtEHpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRaadiamLAN------FYSSGQVCTNGT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 262 YILCSQEMQEQLVPALQNAITRFY-GD--NPQTspNLGRIINQKHFKRLQGLLGCG-----RVAIGGQ------SDEGEr 327
Cdd:PRK13252 289 RVFVQKSIKAAFEARLLERVERIRiGDpmDPAT--NFGPLVSFAHRDKVLGYIEKGkaegaRLLCGGErlteggFANGA- 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569005993 328 YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLAlyaysnnAEVIKQVLAR 393
Cdd:PRK13252 366 FVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLA-------AGVFTADLSR 424
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
116-369 |
2.71e-29 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 119.48 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 116 EPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPEETGQLL--EHK 193
Cdd:cd07116 135 EPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLasSKR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 194 FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNP-CYVDD--NCDPQTVANRVAWFRYF--NAGQTCVAPDYILCSQE 268
Cdd:cd07116 215 IAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPnIFFADvmDADDAFFDKALEGFVMFalNQGEVCTCPSRALIQES 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 269 MQEQLvpaLQNAITRF----YGDNPQTSPNLGRIINQKHFKRLQGLLGCGR-----VAIGGQ-----SDEGERYIAPTVL 334
Cdd:cd07116 295 IYDRF---MERALERVkaikQGNPLDTETMIGAQASLEQLEKILSYIDIGKeegaeVLTGGErnelgGLLGGGYYVPTTF 371
|
250 260 270
....*....|....*....|....*....|....*
gi 569005993 335 VDVQETEpVMQEEIFGPILPLVTVRSLDEAIEFMN 369
Cdd:cd07116 372 KGGNKMR-IFQEEIFGPVLAVTTFKDEEEALEIAN 405
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
112-353 |
6.39e-29 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 118.37 E-value: 6.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 112 FIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAEL-LPQYLDQSCFAVMLGGPEETGQLL 190
Cdd:cd07140 142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELtVKAGFPKGVINILPGSGSLVGQRL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 191 EHKFDY--IFFTGSPRVGKIVMTAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQ 267
Cdd:cd07140 222 SDHPDVrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 268 EMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRL-----QGLLGCGRVAIGG-QSDEGERYIAPTVLVDVQET 340
Cdd:cd07140 302 SIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLveyceRGVKEGATLVYGGkQVDRPGFFFEPTVFTDVEDH 381
|
250
....*....|...
gi 569005993 341 EPVMQEEIFGPIL 353
Cdd:cd07140 382 MFIAKEESFGPIM 394
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
18-418 |
2.09e-27 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 114.21 E-value: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 18 EEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESD--MSEII-LCENEVDLALKNLQTW 94
Cdd:cd07125 72 DAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADaeVREAIdFCRYYAAQARELFSDP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 95 MKDEPVS-TNLLtklstafiRKEPFGLVLIIAPWNYPVNlmiIPL---VGAIAAGNCVVLKPSEISKNTEKVLAELL--- 167
Cdd:cd07125 152 ELPGPTGeLNGL--------ELHGRGVFVCISPWNFPLA---IFTgqiAAALAAGNTVIAKPAEQTPLIAARAVELLhea 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 168 --PQYLDQscfaVMLGGPEETGQ-LLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITL---ELGGKNPCYVDDNCDP-Q 239
Cdd:cd07125 221 gvPRDVLQ----LVPGDGEEIGEaLVAHPrIDGVIFTGSTETAKLINRALAERDGPILPliaETGGKNAMIVDSTALPeQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 240 TVANRVA-WFRyfNAGQTCVAPDyILCSQE-MQEQLVPALQNAITRFYGDNPQT-SPNLGRIINQKHFKRLQGLL----G 312
Cdd:cd07125 297 AVKDVVQsAFG--SAGQRCSALR-LLYLQEeIAERFIEMLKGAMASLKVGDPWDlSTDVGPLIDKPAGKLLRAHTelmrG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 313 CGRVAIGGQSDEGE-RYIAPTVLVDVqeTEPVMQEEIFGPILPLVTVRS--LDEAIEFMNQREKPLALYAYSNNAEVIKQ 389
Cdd:cd07125 374 EAWLIAPAPLDDGNgYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKAedLDEAIEDINATGYGLTLGIHSRDEREIEY 451
|
410 420 430
....*....|....*....|....*....|..
gi 569005993 390 VLARTSSGGFCGNDGfmyMT---LSSLPFGGV 418
Cdd:cd07125 452 WRERVEAGNLYINRN---ITgaiVGRQPFGGW 480
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
117-369 |
1.87e-26 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 111.14 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 117 PFGLVLIIAPWNYPV-----NLMIiplvgAIAAGNCVVLKPSE----ISKNTEKVLAELLPQY-LDQSCFAVMLGGPEET 186
Cdd:cd07130 132 PLGVVGVITAFNFPVavwgwNAAI-----ALVCGNVVVWKPSPttplTAIAVTKIVARVLEKNgLPGAIASLVCGGADVG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 187 GQLLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILC 265
Cdd:cd07130 207 EALVKDPrVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 266 SQEMQEQLVPALQNAITRFYGDNPQTSPNL-GRIINQKHFKRLQGLL------GcGRVAIGGQSDEGE-RYIAPTVlVDV 337
Cdd:cd07130 287 HESIYDEVLERLKKAYKQVRIGDPLDDGTLvGPLHTKAAVDNYLAAIeeaksqG-GTVLFGGKVIDGPgNYVEPTI-VEG 364
|
250 260 270
....*....|....*....|....*....|..
gi 569005993 338 QETEPVMQEEIFGPILPLVTVRSLDEAIEFMN 369
Cdd:cd07130 365 LSDAPIVKEETFAPILYVLKFDTLEEAIAWNN 396
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
16-423 |
4.80e-25 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 107.35 E-value: 4.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 16 PFEEKLQRLkEAFntgktktakfrAEQLQSlgrflqdNSKQLHDALDGDLGKSGFESdMSEIILCENEVDLALKNLQ--T 93
Cdd:PRK09457 57 SFEERQAIV-ERF-----------AALLEE-------NKEELAEVIARETGKPLWEA-ATEVTAMINKIAISIQAYHerT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 94 WMKDEPVSTNlltklsTAFIRKEPFGLVLIIAPWNYPVNL---MIIPlvgAIAAGNCVVLKPSEIsknTEKVlAELLPQY 170
Cdd:PRK09457 117 GEKRSEMADG------AAVLRHRPHGVVAVFGPYNFPGHLpngHIVP---ALLAGNTVVFKPSEL---TPWV-AELTVKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 171 LDQSCF--AV--MLGGPEETGQ-LLEHK-FDYIFFTGSPRVGKIVMTAAAKHLTPI-TLELGGKNPCYVDDNCDPQTVAN 243
Cdd:PRK09457 184 WQQAGLpaGVlnLVQGGRETGKaLAAHPdIDGLLFTGSANTGYLLHRQFAGQPEKIlALEMGGNNPLVIDEVADIDAAVH 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 244 RVAWFRYFNAGQTCVAPDYILCSQEMQ-EQLVPALQNAITRFYGDNP--QTSPNLGRIINQKHFKRL----QGLLGCGRV 316
Cdd:PRK09457 264 LIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWdaEPQPFMGAVISEQAAQGLvaaqAQLLALGGK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 317 AI--GGQSDEGERYIAPTvLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLART 394
Cdd:PRK09457 344 SLleMTQLQAGTGLLTPG-IIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEI 422
|
410 420 430
....*....|....*....|....*....|...
gi 569005993 395 SSGGFCGN---DGfmymTLSSLPFGGV-ASPEH 423
Cdd:PRK09457 423 RAGIVNWNkplTG----ASSAAPFGGVgASGNH 451
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
13-418 |
5.50e-25 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 106.75 E-value: 5.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 13 GTDPFEEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSgFESDMSEIILCENEVDLALKNLQ 92
Cdd:PRK09406 21 TDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LASAKAEALKCAKGFRYYAEHAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 93 TWMKDEPVSTNLLtKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-L 171
Cdd:PRK09406 100 ALLADEPADAAAV-GASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAgF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 172 DQSCFAVMLGGPEETGQLL-EHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRY 250
Cdd:PRK09406 179 PDGCFQTLLVGSGAVEAILrDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 251 FNAGQTCVAPDYILCSQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRLQGLL-----GCGRVAIGGQSDE 324
Cdd:PRK09406 259 QNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALrVGDPTDPDTDVGPLATEQGRDEVEKQVddavaAGATILCGGKRPD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 325 GER-YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGND 403
Cdd:PRK09406 339 GPGwFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFING 418
|
410
....*....|....*..
gi 569005993 404 gfmyMTLS--SLPFGGV 418
Cdd:PRK09406 419 ----MTVSypELPFGGV 431
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
13-418 |
7.26e-25 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 106.48 E-value: 7.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 13 GTDPFEEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESdMSEIILCENEVDLALKNLQ 92
Cdd:PRK13968 27 GADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA-RAEVAKSANLCDWYAEHGP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 93 TWMKDEPVstnlLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQY-L 171
Cdd:PRK13968 106 AMLKAEPT----LVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAgI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 172 DQSCFAVMLGGPEETGQLL-EHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRY 250
Cdd:PRK13968 182 PQGVYGWLNADNDGVSQMInDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 251 FNAGQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPN-LGRI----INQKHFKRLQGLLGCG-RVAIGGQSDE 324
Cdd:PRK13968 262 QNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENaLGPMarfdLRDELHHQVEATLAEGaRLLLGGEKIA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 325 GE-RYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSG-----G 398
Cdd:PRK13968 342 GAgNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGgvfinG 421
|
410 420
....*....|....*....|
gi 569005993 399 FCGNDgfmymtlSSLPFGGV 418
Cdd:PRK13968 422 YCASD-------ARVAFGGV 434
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
105-369 |
2.46e-24 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 104.81 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 105 LTKLST---AFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAEL-----LPQyldQSCF 176
Cdd:cd07148 109 LTPASAgriAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLlheagLPE---GWCQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 177 AVMLGGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHlTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQT 256
Cdd:cd07148 186 AVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 257 CVAPDYILCSQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFKRL-----QGLLGCGRVAIGGQSdEGERYIA 330
Cdd:cd07148 265 CVSVQRVFVPAEIADDFAQRLAAAAEKLvVGDPTDPDTEVGPLIRPREVDRVeewvnEAVAAGARLLCGGKR-LSDTTYA 343
|
250 260 270
....*....|....*....|....*....|....*....
gi 569005993 331 PTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMN 369
Cdd:cd07148 344 PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQAN 382
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
116-417 |
1.00e-21 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 97.29 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 116 EPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSE-ISKNTEKVLAELLPQYLDQSCFAVMLGGPEETGQLL--EH 192
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEqTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALtsDP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 193 KFDYIFFTGSPRVGKIVMTAAAKHL---TPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEM 269
Cdd:TIGR01238 239 RIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDV 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 270 QEQLVPALQNAITRFYGDNP-QTSPNLGRIIN----QKHFKRLQGLLGCGRV---AIGGQSDEGER--YIAPTV--LVDV 337
Cdd:TIGR01238 319 ADRVLTMIQGAMQELKVGVPhLLTTDVGPVIDaeakQNLLAHIEHMSQTQKKiaqLTLDDSRACQHgtFVAPTLfeLDDI 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 338 QEtepvMQEEIFGPILPLVTVRS--LDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLSSLPF 415
Cdd:TIGR01238 399 AE----LSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPF 474
|
..
gi 569005993 416 GG 417
Cdd:TIGR01238 475 GG 476
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
115-369 |
3.16e-21 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 95.98 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 115 KEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSeisknTEKVLAELLPqyldQSCFAvMLGGPEETGQLLEHKF 194
Cdd:PLN00412 156 KIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPP-----TQGAVAALHM----VHCFH-LAGFPKGLISCVTGKG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 195 DYI--FFTGSPRVGKIVMT------AAAKH--LTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYIL 264
Cdd:PLN00412 226 SEIgdFLTMHPGVNCISFTggdtgiAISKKagMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 265 CSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGGQSDEGER---YIAPTVLVDVQETE 341
Cdd:PLN00412 306 VMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKRegnLIWPLLLDNVRPDM 385
|
250 260
....*....|....*....|....*...
gi 569005993 342 PVMQEEIFGPILPLVTVRSLDEAIEFMN 369
Cdd:PLN00412 386 RIAWEEPFGPVLPVIRINSVEEGIHHCN 413
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
17-401 |
7.41e-21 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 94.90 E-value: 7.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 17 FEEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFES--DMSEII-LCENEVDLAlknlqt 93
Cdd:PLN02315 58 YEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGigEVQEIIdMCDFAVGLS------ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 94 wmkdepvstnllTKLSTAFIRKE-----------PFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLK--PSE--ISKN 158
Cdd:PLN02315 132 ------------RQLNGSIIPSErpnhmmmevwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKgaPTTplITIA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 159 TEKVLAELLPQY-LDQSCFAVMLGGPEeTGQLL--EHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDN 235
Cdd:PLN02315 200 MTKLVAEVLEKNnLPGAIFTSFCGGAE-IGEAIakDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 236 CDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKR--LQGLLGC 313
Cdd:PLN02315 279 ADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKnfEKGIEII 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 314 ----GRVAIGGQSDEGE-RYIAPTVlVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIK 388
Cdd:PLN02315 359 ksqgGKILTGGSAIESEgNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIF 437
|
410
....*....|...
gi 569005993 389 QVLARTSSGgfCG 401
Cdd:PLN02315 438 KWIGPLGSD--CG 448
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
117-398 |
6.44e-17 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 82.67 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 117 PFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQ--YLDQSCFAVMLGGPEETGQLLEH-K 193
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDVTLINGDGKTMQALLLHpN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 194 FDYIFFTGSPRVGKIVmtAAAKHLTPITLELGGKNPCYVDDNCDP-QTVANRVAWFRYFNAGQTCVAPDYILCSQEMQEQ 272
Cdd:cd07084 180 PKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQAvDYVAWQCVQDMTACSGQKCTAQSMLFVPENWSKT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 273 -LVPALQNAITRfygDNPQTSpNLGRIINQKHFKRLQGLLG-CGRVAIGGQSDEGERYI--------APTVLVDVQE--- 339
Cdd:cd07084 258 pLVEKLKALLAR---RKLEDL-LLGPVQTFTTLAMIAHMENlLGSVLLFSGKELKNHSIpsiygacvASALFVPIDEilk 333
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569005993 340 TEPVMQEEIFGPILPLVTVRSLDEA--IEFMNQREKPLALYAYSNNAEVIKQVLARTSSGG 398
Cdd:cd07084 334 TYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAG 394
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
115-398 |
9.15e-16 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 79.41 E-value: 9.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 115 KEPFGLVLIIAPWNYP--VNLMIIPLvgAIAAGNCVVLKPSEISKNTEKVLAEL-LPQYLDQSCFAVMLGGPEETGQLLE 191
Cdd:PLN02419 247 REPLGVCAGICPFNFPamIPLWMFPV--AVTCGNTFILKPSEKDPGASVILAELaMEAGLPDGVLNIVHGTNDTVNAICD 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 192 HK-FDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILC---SQ 267
Cdd:PLN02419 325 DEdIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAK 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 268 EMQEQLVPALQnAITRFYGDNPQTspNLGRIINQKHFKRLQGLLGCG-----RVAIGGQS-----DEGERYIAPTVLVDV 337
Cdd:PLN02419 405 SWEDKLVERAK-ALKVTCGSEPDA--DLGPVISKQAKERICRLIQSGvddgaKLLLDGRDivvpgYEKGNFIGPTILSGV 481
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569005993 338 QETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREkplalyaYSNNAEVIkqvlarTSSGG 398
Cdd:PLN02419 482 TPDMECYKEEIFGPVLVCMQANSFDEAISIINKNK-------YGNGAAIF------TSSGA 529
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
117-390 |
6.33e-14 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 73.67 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 117 PFGLVLIIA-----PWN-YPvnlmiiPLVGAIAAGNCVVLKPSEIS--------KNTEKVLAELlpqYLDQSCFAVMLGG 182
Cdd:cd07127 193 PRGVALVIGcstfpTWNgYP------GLFASLATGNPVIVKPHPAAilplaitvQVAREVLAEA---GFDPNLVTLAADT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 183 PEE--TGQLLEH-KFDYIFFTGSPRVGKIVMTAAAKHLtpITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVA 259
Cdd:cd07127 264 PEEpiAQTLATRpEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTT 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 260 PDYILCS----QEMQEQLVP-----ALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGGQSDE-----G 325
Cdd:cd07127 342 PQNIYVPrdgiQTDDGRKSFdevaaDLAAAIDGLLADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAhpefpD 421
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569005993 326 ERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQ--REK-PLALYAYSNNAEVIKQV 390
Cdd:cd07127 422 ARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvREHgAMTVGVYSTDPEVVERV 489
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
116-369 |
1.27e-13 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 73.36 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 116 EPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEiskNTEKVLAEllpqyldqscfAVML----GGPEETGQLLE 191
Cdd:PRK11905 675 KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAE---QTPLIAAR-----------AVRLlheaGVPKDALQLLP 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 192 HKFDYI-------------FFTGSPRVGKIVMTAAAKHLTPITL---ELGGKNPCYVDDNCDP-QTVANRVA-WFRyfNA 253
Cdd:PRK11905 741 GDGRTVgaalvadpriagvMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAMIVDSSALPeQVVADVIAsAFD--SA 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 254 GQTCVAPDyILCSQE-----MQEQLVPALQNAITrfyGDNPQTSPNLGRIINQK-------HFKRLQGLlGCG--RVAIG 319
Cdd:PRK11905 819 GQRCSALR-VLCLQEdvadrVLTMLKGAMDELRI---GDPWRLSTDVGPVIDAEaqanieaHIEAMRAA-GRLvhQLPLP 893
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 569005993 320 GQSDEGeRYIAPTVLvdvqETE--PVMQEEIFGPILPLVTVRS--LDEAIEFMN 369
Cdd:PRK11905 894 AETEKG-TFVAPTLI----EIDsiSDLEREVFGPVLHVVRFKAdeLDRVIDDIN 942
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
141-372 |
1.28e-13 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 72.57 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 141 AIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQS-----CFAVMLGGPEETGQ-LLEH-KFDYIFFTGSPRVGKIVMTAA 213
Cdd:cd07129 131 ALAAGCPVVVKAHPAHPGTSELVARAIRAALRATglpagVFSLLQGGGREVGVaLVKHpAIKAVGFTGSRRGGRALFDAA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 214 AKHLTPIT--LELGGKNPCYVDdncdPQTVANR--------VAWFRyFNAGQTCVAPDYIL-----CSQEMQEQLVPALQ 278
Cdd:cd07129 211 AARPEPIPfyAELGSVNPVFIL----PGALAERgeaiaqgfVGSLT-LGAGQFCTNPGLVLvpagpAGDAFIAALAEALA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 279 NAitrfygdNPQT--SPNLgriinQKHFK----RLQGLLGcGRVAIGGQSDEGERYIAPTVL-VDVQE--TEPVMQEEIF 349
Cdd:cd07129 286 AA-------PAQTmlTPGI-----AEAYRqgveALAAAPG-VRVLAGGAAAEGGNQAAPTLFkVDAAAflADPALQEEVF 352
|
250 260
....*....|....*....|...
gi 569005993 350 GPILPLVTVRSLDEAIEFMNQRE 372
Cdd:cd07129 353 GPASLVVRYDDAAELLAVAEALE 375
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
117-417 |
2.71e-13 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 72.31 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 117 PFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSE----ISKNTEKVLAE---------LLPqyldqscfavmlGGP 183
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEqtplIAAQAVRILLEagvpagvvqLLP------------GRG 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 184 EETGQLL--EHKFDYIFFTGSPRVGKIVMTAAAKHL------TPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQ 255
Cdd:PRK11809 836 ETVGAALvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQ 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 256 TCVAPDyILCSQE-MQEQLVPALQNAITRFYGDNP-QTSPNLGRIIN-------QKHfkrLQGLLGCGRV---AIGGQSD 323
Cdd:PRK11809 916 RCSALR-VLCLQDdVADRTLKMLRGAMAECRMGNPdRLSTDIGPVIDaeakaniERH---IQAMRAKGRPvfqAARENSE 991
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 324 EGER--YIAPTV--LVDVQEtepvMQEEIFGPILPLVTVRS--LDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSG 397
Cdd:PRK11809 992 DWQSgtFVPPTLieLDSFDE----LKREVFGPVLHVVRYNRnqLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVG 1067
|
330 340
....*....|....*....|
gi 569005993 398 GFCGNDGFMYMTLSSLPFGG 417
Cdd:PRK11809 1068 NLYVNRNMVGAVVGVQPFGG 1087
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
119-403 |
6.01e-12 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 67.23 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 119 GLVLIIAPWNYPvnlmiiplvgAIAA---------GNCVVLKPSE--ISKN--TEKVLAEL-LPQYLDQscFaVMLGGPE 184
Cdd:cd07123 172 GFVYAVSPFNFT----------AIGGnlagapalmGNVVLWKPSDtaVLSNylVYKILEEAgLPPGVIN--F-VPGDGPV 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 185 ETGQLLEHK-FDYIFFTGSPRVGKIVMTAAAKHLT-----P-ITLELGGKNPCYVDDNCDPQTVAN---RVAwFRYfnAG 254
Cdd:cd07123 239 VGDTVLASPhLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTatvRGA-FEY--QG 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 255 QTCVA------PDYILcsQEMQEQLVPALQnAITrfYGDNPQTSPNLGRIINQKHFKRLQGLLGCGR------VAIGGQS 322
Cdd:cd07123 316 QKCSAasrayvPESLW--PEVKERLLEELK-EIK--MGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKsdpeaeIIAGGKC 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 323 DEGERY-IAPTVLVDVQETEPVMQEEIFGPILplvTVRSLDEAiEFmnqrEKPLAL------YA-----YSNNAEVIKQV 390
Cdd:cd07123 391 DDSVGYfVEPTVIETTDPKHKLMTEEIFGPVL---TVYVYPDS-DF----EETLELvdttspYAltgaiFAQDRKAIREA 462
|
330
....*....|....*
gi 569005993 391 LA--RTSSGGFCGND 403
Cdd:cd07123 463 TDalRNAAGNFYIND 477
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
113-397 |
6.67e-12 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 67.92 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 113 IRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEiskNTEKVLAEllpqyldqscfAVML----GGPEETGQ 188
Cdd:PRK11904 680 LRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAE---QTPLIAAE-----------AVKLlheaGIPKDVLQ 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 189 LL-------------EHKFDYIFFTGSPRVGKIV-MTAAAKHLTPITL--ELGGKNPCYVDDNCDPQTVANRV---AwFR 249
Cdd:PRK11904 746 LLpgdgatvgaaltaDPRIAGVAFTGSTETARIInRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVvtsA-FR 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 250 yfNAGQTCVAPDyILCSQE-----MQEQLVPALQN-AItrfyGDNPQTSPNLGRIINQKHFKRLQ---------GLLGCg 314
Cdd:PRK11904 825 --SAGQRCSALR-VLFVQEdiadrVIEMLKGAMAElKV----GDPRLLSTDVGPVIDAEAKANLDahiermkreARLLA- 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 315 RVAIGGQSDEGErYIAPTvLVDVQETEpVMQEEIFGPILPLVTVRS--LDEAIEFMNQREKPLALYAYSNNAEVIKQVLA 392
Cdd:PRK11904 897 QLPLPAGTENGH-FVAPT-AFEIDSIS-QLEREVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIAD 973
|
....*
gi 569005993 393 RTSSG 397
Cdd:PRK11904 974 RVRVG 978
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
117-366 |
3.34e-10 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 61.48 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 117 PFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSC----FAVMLGGP--EETGQLL 190
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGgpdnLVVTVEEPtiETTNELM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 191 EH-KFDYIFFTGSPRVGKIVMTAAAKhltpiTLELGGKNP-CYVDDNCDPQTVANRVAWFRYFNAGQTC----------- 257
Cdd:cd07121 177 AHpDINLLVVTGGPAVVKAALSSGKK-----AIGAGAGNPpVVVDETADIEKAARDIVQGASFDNNLPCiaekeviavds 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 258 VAPD----------YILCSQEMQEQLVPALQNaitrfygdnpqtspNLGRIINQKHF-KRLQGLLGcgrvAIGGQSDEGE 326
Cdd:cd07121 252 VADYliaamqrngaYVLNDEQAEQLLEVVLLT--------------NKGATPNKKWVgKDASKILK----AAGIEVPADI 313
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 569005993 327 RYIaptvLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIE 366
Cdd:cd07121 314 RLI----IVETDKDHPFVVEEQMMPILPVVRVKNFDEAIE 349
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
116-407 |
1.31e-08 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 56.89 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 116 EPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYldqscfAVMLGGPE----------- 184
Cdd:cd07081 94 EPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQA------AVAAGAPEnligwidnpsi 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 185 ETGQLLEHK--FDYIFFTGSPRVGKivmtAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGqtcvapdy 262
Cdd:cd07081 168 ELAQRLMKFpgIGLLLATGGPAVVK----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNG-------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 263 ILCSQEMQEQLVPALQNAITRFYGDNPqtspnlGRIINQKHFKRLQGLL---GCGRVAIGGQSdegERYIAPTVLVDVQE 339
Cdd:cd07081 236 VICASEQSVIVVDSVYDEVMRLFEGQG------AYKLTAEELQQVQPVIlknGDVNRDIVGQD---AYKIAAAAGLKVPQ 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569005993 340 TEPVMqeeifgpilpLVTVRSLDEAIEFMNQREKP-LALYAYSNNAEVIKQVLARTSSGGfCGNDGFMY 407
Cdd:cd07081 307 ETRIL----------IGEVTSLAEHEPFAHEKLSPvLAMYRAANFADADAKALALKLEGG-CGHTSAMY 364
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
116-393 |
1.30e-07 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 54.17 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 116 EPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSE-----------------ISKNtekVLAeLLPqyldqscfav 178
Cdd:COG4230 679 RGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEqtpliaaravrllheagVPAD---VLQ-LLP---------- 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 179 mlGGPEETGQLL--EHKFDYIFFTGSPRVGKIV-MTAAAKHLTPITL--ELGGKNPCYVDDNCDPQTVANRV---AwFRy 250
Cdd:COG4230 745 --GDGETVGAALvaDPRIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGGQNAMIVDSSALPEQVVDDVlasA-FD- 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 251 fNAGQTCVAPDyILCSQE-------------MQEQLVpalqnaitrfyGDNPQTSPNLGRIIN-------QKHFKRLQ-- 308
Cdd:COG4230 821 -SAGQRCSALR-VLCVQEdiadrvlemlkgaMAELRV-----------GDPADLSTDVGPVIDaearanlEAHIERMRae 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 309 GLLgCGRVAIGGQSDEGeRYIAPTV--LVDVQEtepvMQEEIFGPILPLVTVRS--LDEAIEFMNQREKPLALYAYSNNA 384
Cdd:COG4230 888 GRL-VHQLPLPEECANG-TFVAPTLieIDSISD----LEREVFGPVLHVVRYKAdeLDKVIDAINATGYGLTLGVHSRID 961
|
....*....
gi 569005993 385 EVIKQVLAR 393
Cdd:COG4230 962 ETIDRVAAR 970
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
117-397 |
2.68e-07 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 52.88 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 117 PFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLK-PSEISKNTEKVLAEL----LPQyldQSCFAVMLGGPEETGQLLE 191
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKvDSKVSVVMEQFLRLLhlcgMPA---TDVDLIHSDGPTMNKILLE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 192 HKFDYIFFTGSPRV---------GKIVMTAAA---KHLTPITLELGgknpcYVDDNCDPQTvanrvawfrYFNAGQTCVA 259
Cdd:cd07126 219 ANPRMTLFTGSSKVaerlalelhGKVKLEDAGfdwKILGPDVSDVD-----YVAWQCDQDA---------YACSGQKCSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 260 PDyILCSQE--MQEQLVPALQNAITRFYGDNPQTSPNLG----RIINqkHFKRLQGLLGcGRVAIGGQSDEGERYIA--- 330
Cdd:cd07126 285 QS-ILFAHEnwVQAGILDKLKALAEQRKLEDLTIGPVLTwtteRILD--HVDKLLAIPG-AKVLFGGKPLTNHSIPSiyg 360
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569005993 331 ---------PTVLVDVQETEPVMQEEIFGP--ILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSG 397
Cdd:cd07126 361 ayeptavfvPLEEIAIEENFELVTTEVFGPfqVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNG 438
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
119-391 |
3.25e-06 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 49.19 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 119 GLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKP-SEISKNTEKVLAE-----LLPQyldqSCFAVMLGGpeeTGQLLEH 192
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPaTATAYLTEAVVKDivesgLLPE----GALQLICGS---VGDLLDH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 193 --KFDYIFFTGSPRVGKIVMT--AAAKHLTPITLELGGKNPCYVDDNCDPQT-----VANRVAWFRYFNAGQTCVAPDYI 263
Cdd:cd07128 219 lgEQDVVAFTGSAATAAKLRAhpNIVARSIRFNAEADSLNAAILGPDATPGTpefdlFVKEVAREMTVKAGQKCTAIRRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 264 LCSQEMQEQLVPALQNAITRF-YGDNPQTSPNLGRIIN--QKH--FKRLQGLLGCGRVAIGGQSD--------EGERYIA 330
Cdd:cd07128 299 FVPEARVDAVIEALKARLAKVvVGDPRLEGVRMGPLVSreQREdvRAAVATLLAEAEVVFGGPDRfevvgadaEKGAFFP 378
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569005993 331 PTVLV--DVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVL 391
Cdd:cd07128 379 PTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
117-366 |
3.58e-05 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 46.05 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 117 PFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSC----FAVMLGGP--EETGQLL 190
Cdd:PRK15398 129 PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVAAGgpenLVVTVAEPtiETAQRLM 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 191 EH-KFDYIFFTGSPRVGKIVMTAAAKhltpiTLELGGKNP-CYVDDNCDPQTVANRVAWFRYFNAGQTCVAP-------- 260
Cdd:PRK15398 209 KHpGIALLVVTGGPAVVKAAMKSGKK-----AIGAGAGNPpVVVDETADIEKAARDIVKGASFDNNLPCIAEkevivvds 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 261 --DYILcsQEMQE----QLVPALQNAITRFygdnpqtspnlgrIINQKHF--KRLQG-----LLGcgrvAIGGQSDEGER 327
Cdd:PRK15398 284 vaDELM--RLMEKngavLLTAEQAEKLQKV-------------VLKNGGTvnKKWVGkdaakILE----AAGINVPKDTR 344
|
250 260 270
....*....|....*....|....*....|....*....
gi 569005993 328 YIaptvLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIE 366
Cdd:PRK15398 345 LL----IVETDANHPFVVTELMMPVLPVVRVKDVDEAIA 379
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
26-245 |
7.70e-05 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 44.91 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 26 EAFNTGK----TKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLG---KSGFESDMSEIILCENEV-DLALKNLQTWMKD 97
Cdd:cd07077 1 ESAKNAQrtlaVNHDEQRDLIINAIANALYDTRQRLASEAVSERGayiRSLIANWIAMMGCSESKLyKNIDTERGITASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 98 EPVSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVnLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQyldqscfA 177
Cdd:cd07077 81 GHIQDVLLPDNGETYVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQA-------A 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569005993 178 VMLGGPEETGQLLEH-------------KFDYIFFTGSPRVGKivmtAAAKHLTPITLeLG---GKNPCYVDDNCDPQTV 241
Cdd:cd07077 153 DAAHGPKILVLYVPHpsdelaeellshpKIDLIVATGGRDAVD----AAVKHSPHIPV-IGfgaGNSPVVVDETADEERA 227
|
....
gi 569005993 242 ANRV 245
Cdd:cd07077 228 SGSV 231
|
|
| |
